HMGA2 Protein
HMGA1a Protein
HMGA1b Protein
AT-Hook Motifs
HMGA1c Protein
Lipoma
Homogentisate 1,2-Dioxygenase
Specific binding of high-mobility-group I (HMGI) protein and histone H1 to the upstream AT-rich region of the murine beta interferon promoter: HMGI protein acts as a potential antirepressor of the promoter. (1/192)
The high-mobility-group I (HMGI) protein is a nonhistone component of active chromatin. In this work, we demonstrate that HMGI protein specifically binds to the AT-rich region of the murine beta interferon (IFN-beta) promoter localized upstream of the murine virus-responsive element (VRE). Contrary to what has been described for the human promoter, HMGI protein did not specifically bind to the VRE of the murine IFN-beta promoter. Stably transfected promoters carrying mutations on this HMGI binding site displayed delayed virus-induced kinetics of transcription. When integrated into chromatin, the mutated promoter remained repressed and never reached normal transcriptional activity. Such a phenomenon was not observed with transiently transfected promoters upon which chromatin was only partially reconstituted. Using UV footprinting, we show that the upstream AT-rich sequences of the murine IFN-beta promoter constitute a preferential binding region for histone H1. Transfection with a plasmid carrying scaffold attachment regions as well as incubation with distamycin led to the derepression of the IFN-beta promoter stably integrated into chromatin. In vitro, HMGI protein was able to displace histone H1 from the upstream AT-rich region of the wild-type promoter but not from the promoter carrying mutations on the upstream high-affinity HMGI binding site. Our results suggest that the binding of histone H1 to the upstream AT-rich region of the promoter might be partly responsible for the constitutive repression of the promoter. The displacement by HMGI protein of histone H1 could help to convert the IFN-beta promoter from a repressed to an active state. (+info)High mobility group-I(Y) protein facilitates nuclear factor-kappaB binding and transactivation of the inducible nitric-oxide synthase promoter/enhancer. (2/192)
Nitric oxide (NO), a free radical gas whose production is catalyzed by the enzyme NO synthase, participates in the regulation of multiple organ systems. The inducible isoform of NO synthase (iNOS) is transcriptionally up-regulated by inflammatory stimuli; a critical mediator of this process is nuclear factor (NF)-kappaB. Our objective was to determine which regulatory elements other than NF-kappaB binding sites are important for activation of the iNOS promoter/enhancer. We also wanted to identify transcription factors that may be functioning in conjunction with NF-kappaB (subunits p50 and p65) to drive iNOS transcription. Deletion analysis of the iNOS promoter/enhancer revealed that an AT-rich sequence (-61 to -54) downstream of the NF-kappaB site (-85 to -76) in the 5'-flanking sequence was important for iNOS induction by interleukin-1beta and endotoxin in vascular smooth muscle cells. This AT-rich sequence, corresponding to an octamer (Oct) binding site, bound the architectural transcription factor high mobility group (HMG)-I(Y) protein. Electrophoretic mobility shift assays showed that HMG-I(Y) and NF-kappaB subunit p50 bound to the iNOS promoter/enhancer to form a ternary complex. The formation of this complex required HMG-I(Y) binding at the Oct site. The location of an HMG-I(Y) binding site typically overlaps that of a recruited transcription factor. In the iNOS promoter/enhancer, however, HMG-I(Y) formed a complex with p50 while binding downstream of the NF-kappaB site. Furthermore, overexpression of HMG-I(Y) potentiated iNOS promoter/enhancer activity by p50 and p65 in transfection experiments, suggesting that HMG-I(Y) contributes to the transactivation of iNOS by NF-kappaB. (+info)The host-cell architectural protein HMG I(Y) modulates binding of herpes simplex virus type 1 ICP4 to its cognate promoter. (3/192)
The productive infection cycle of herpes simplex virus is controlled in part by the action of ICP4, an immediate-early gene product that acts as both an activator and repressor of transcription. ICP4 is autoregulatory, and IE-3, the gene that encodes it, contains a high-affinity binding site for the protein at its cap site. Previously, we had demonstrated that this site could be occupied by proteins found in nuclear extracts from uninfected cells. A HeLa cell cDNA expression library was screened with a DNA probe containing the IE-3 gene cap site, and clones expressing the architectural chromatin proteins HMG I and HMG Y were identified by this technique. HMG I is shown to augment binding of ICP4 to its cognate site in in vitro assays and to enhance the activity of this protein in short-term transient expression assays. (+info)Determination of high mobility group I(Y) expression level in colorectal neoplasias: a potential diagnostic marker. (4/192)
High mobility group I(Y) [HMGI(Y)] proteins are architectural factors abundantly expressed during embryogenesis, and their overexpression is known to be closely associated with neoplastic transformation of cells. This study was performed to investigate whether determination of HMGI(Y) expression level could assist in (a) differential diagnosis between colorectal carcinoma, adenoma, and normal tissue and (b) determination of the prognosis of patients with colorectal cancer. To this end, HMGI(Y) expression was determined at both the protein and mRNA levels in 30 colorectal carcinomas, 26 adenomas, and 23 normal mucosa samples, and further correlations between the protein expression levels and various clinicopathological parameters, such as depth of tumor invasion, lymphatic and/or venous involvement, regional lymph node metastasis, and Dukes' stage, were determined in 30 carcinoma cases. The expression of HMGI(Y) proteins was significantly increased in carcinoma and adenoma with severe atypia compared with that in adenoma with less atypia and normal colorectal mucosa. This increase in HMGI(Y) protein expression was found to be because of an increase in its mRNA expression by RNA in situ hybridization analysis. Clinicopathological analysis revealed that the level of HMGI(Y) protein expression was significantly correlated with parameters known to be indicative of a poor prognosis in colorectal cancer patients. These findings indicate that the determination of the HMGI(Y) protein expression level could be a potential marker for the diagnosis of colorectal neoplasias and can be of great value in predicting the prognosis of patients with colorectal cancer. (+info)Directional binding of HMG-I(Y) on four-way junction DNA and the molecular basis for competitive binding with HMG-1 and histone H1. (5/192)
Histone H1, HMG-1 and HMG-I(Y) are mammalian nuclear proteins possessing distinctive DNA-binding domain structures that share the common property of preferentially binding to four-way junction (4H) DNA, an in vitro mimic of the in vivo genetic recombination intermediate known as the Holliday junction. Nevertheless, these three proteins bind to 4H DNA in vitro with very different affinities and in a mutually exclusive manner. To investigate the molecular basis for these distinctive binding characteristics, we employed base pair resolution hydroxyl radical footprinting to determine the precise sites of nucleotide interactions of both HMG-1 and histone H1 on 4H DNA and compared these contacts with those previously described for HMG-I(Y) on the same substrate. Each of these proteins had a unique binding pattern on 4H DNA and yet shared certain common nucleotide contacts on the arms of the 4H DNA molecule near the branch point. Both the HMG-I(Y) and HMG-1 proteins made specific contacts across the 4H DNA branch point, as well as interacting at discrete sites on the arms, whereas the globular domain of histone H1 bound exclusively to the arms of the 4H DNA substrate without contacting nucleotides at the crossover region. Experiments employing the chemical cleavage reagent 1, 10-orthophenanthroline copper(II) attached to the C-terminal end of a site-specifically mutagenized HMG-I(Y) protein molecule demonstrated that this protein binds to 4H DNA in a distinctly polar, direction-specific manner. Together these results provide an attractive molecular explanation for the observed mutually exclusive 4H DNA-binding characteristics of these proteins and also allow for critical assessment of proposed models for their interaction with 4H DNA substrates. The results also have important implications concerning the possible in vivo roles of HMG-I(Y), histone H1 and HMG-1 in biological processes such as genetic recombination and retroviral integration. (+info)HMGI(Y) and HMGI-C genes are expressed in neuroblastoma cell lines and tumors and affect retinoic acid responsiveness. (6/192)
HMGI-C and HMGI(Y) are architectural DNA-binding proteins that participate in the conformational regulation of active chromatin. Their pattern of expression in embryonal and adult tissues, the analysis of the "pygmy" phenotype induced by the inactivation of the HMGI-C gene, and their frequent qualitative or quantitative alteration in experimental and human tumors indicate their pivotal role in the control of cell growth, differentiation, and tumorigenesis in several tissues representative of the epithelial, mesenchymal, and hematopoietic lineages. In contrast, very little information is available on their expression and function in neural cells. Here, we investigated the expression of the HMGI(Y) and HMGI-C genes in neuroblastoma (NB), a tumor arising from an alteration of the normal differentiation of neural crest-derived cells and in embryonal and adult adrenal tissue. Although HMGI(Y) is constitutively expressed in the embryonal and adult adrenal gland and in all of the NB cell lines and ex vivo tumors examined, its regulation appears to be associated to growth inhibition and differentiation because we observed that HMGI(Y) expression is reduced by retinoic acid (RA) in several NB cell lines that are induced to differentiate into postmitotic neurons, whereas it is up-regulated by RA in cells that fail to differentiate. Furthermore, the decrease of HMGI(Y) expression observed in RA-induced growth arrest and differentiation is abrogated in cells that have been made insensitive to this drug by NMYC overexpression. In contrast, HMGI-C expression is down-regulated during the development of the adrenal gland, completely absent in the adult individual, and only detectable in a subset of ex vivo NB tumors and in RA-resistant NB cell lines. We provide evidence of a causal link between HMGI-C expression and resistance to the growth arrest induced by RA in NB cell lines because exogenous HMGI-C expression in HMGI-C-negative and RA-sensitive cells is sufficient to convert them into RA-resistant cells. Therefore, we suggest that HMGI-C and HMGI(Y) may participate in growth- and differentiation-related tumor progression events of neuroectodermal derivatives. (+info)The HMG-I(Y) A.T-hook peptide motif confers DNA-binding specificity to a structured chimeric protein. (7/192)
Chromosomal translocations involving genes coding for members of the HMG-I(Y) family of "high mobility group" non-histone chromatin proteins (HMG-I, HMG-Y, and HMG-IC) have been observed in numerous types of human tumors. Many of these gene rearrangements result in the creation of chimeric proteins in which the DNA-binding domains of the HMG-I(Y) proteins, the so-called A.T-hook motifs, have been fused to heterologous peptide sequences. Although little is known about either the structure or biophysical properties of these naturally occurring fusion proteins, the suggestion has been made that such chimeras have probably assumed an altered in vivo DNA-binding specificity due to the presence of the A.T-hook motifs. To investigate this possibility, we performed in vitro "domain-swap" experiments using a model protein fusion system in which a single A. T-hook peptide was exchanged for a corresponding length peptide in the well characterized "B-box" DNA-binding domain of the HMG-1 non-histone chromatin protein. Here we report that chimeric A. T-hook/B-box hybrids exhibit in vitro DNA-binding characteristics resembling those of wild type HMG-I(Y) protein, rather than the HMG-1 protein. These results strongly suggest that the chimeric fusion proteins produced in human tumors as a result of HMG-I(Y) gene chromosomal translocations also retain A.T-hook-imparted DNA-binding properties in vivo. (+info)The role of HMG I(Y) in the assembly and function of the IFN-beta enhanceosome. (8/192)
Transcriptional activation of the virus inducible enhancer of the human interferon-beta (IFN-beta) gene in response to virus infection requires the assembly of an enhanceosome, consisting of the transcriptional activators NF-kappaB, ATF-2/c-Jun, IRFs and the architectural protein of the mammalian high mobility group I(Y) [HMG I(Y)]. Here, we demonstrate that the first step in enhanceosome assembly, i.e. HMG I(Y)-dependent recruitment of NF-kappaB and ATF-2/c-Jun to the enhancer, is facilitated by discrete regions of HMG I and is mediated by allosteric changes induced in the DNA by HMG I(Y) and not by protein-protein interactions between HMG I(Y) and these proteins. However, we show that completion of the enhanceosome assembly process requires protein-protein interactions between HMG I(Y) and the activators. Finally, we demonstrate that once assembled, the IFN-beta enhanceosome is an unusually stable nucleoprotein structure that can activate transcription at high levels by promoting multiple rounds of reinitiation of transcription. (+info)High Mobility Group AT-Hook 2 (HMGA2) protein is a non-histone chromatin protein that belongs to the HMGA family. This protein contains structural DNA-binding domains called AT-hooks, which allow it to bind to the minor groove of AT-rich sequences in the promoter or enhancer regions of genes.
HMGA2 protein plays a crucial role in regulating gene transcription, chromatin architecture, and nuclear organization during development and differentiation. It is involved in various cellular processes such as proliferation, apoptosis, and senescence. Moreover, HMGA2 has been implicated in several human diseases, including cancer, where its overexpression is often associated with poor prognosis and aggressive tumor behavior.
In summary, HMGA2 protein is a DNA-binding protein that regulates gene expression and is involved in development, differentiation, and disease, particularly cancer.
High Mobility Group AT-Hook 1 (HMGA1) is a non-histone chromosomal protein that belongs to the HMGA family. The HMGA proteins are characterized by their ability to bind to AT-rich regions in the minor groove of DNA and modulate the chromatin structure, thereby regulating gene transcription.
The HMGA1 protein exists in two isoforms, HMGA1a and HMGA1b, which differ in their amino acid sequences due to alternative splicing of the HMGA1 pre-mRNA. The HMGA1a isoform has 108 amino acids, while HMGA1b has 109 amino acids.
HMGA1 proteins play crucial roles in various cellular processes, including proliferation, differentiation, and apoptosis. Dysregulation of HMGA1 expression has been implicated in several human diseases, such as cancer, where it functions as a transcriptional regulator of genes involved in tumorigenesis.
High Mobility Group AT-Hook 1b (HMGA1b) protein is a subtype of the HMGA1 protein, which belongs to the High Mobility Group AT-hook (HMGA) family of non-histone chromatin proteins. These proteins are characterized by their ability to bind to the minor groove of AT-rich DNA sequences and modulate chromatin structure and gene expression.
The HMGA1 protein exists in two isoforms, HMGA1a and HMGA1b, which are generated through alternative splicing of the same gene. Both isoforms share a similar structure, consisting of three AT-hook DNA binding domains and a C-terminal acidic tail. However, they differ in their N-terminal regions, with HMGA1b having a unique 29-amino acid sequence that is not present in HMGA1a.
HMGA1 proteins play important roles in various cellular processes, including transcription regulation, DNA replication, and repair. Dysregulation of HMGA1 expression has been implicated in several human diseases, such as cancer, where it can act as a potent oncogene by promoting tumor cell proliferation, migration, and invasion.
AT-hook motifs are short DNA-binding domains that are found in many eukaryotic transcription factors and other proteins that interact with chromatin. These motifs are typically composed of 6-8 amino acid residues, characterized by the presence of a highly conserved tripeptide sequence (PWK, PWV, or PWY), which is responsible for their ability to bind to the minor groove of AT-rich DNA sequences.
The AT-hook motifs can bend and kink the DNA helix, leading to changes in chromatin structure and modulation of gene expression. They play important roles in various nuclear processes, including transcriptional regulation, DNA replication, and repair. The presence of multiple AT-hook motifs in a single protein can enhance its DNA-binding affinity and specificity, allowing it to interact with specific regulatory elements in the genome.
High Mobility Group AT-Hook 1 (HMGA1) is a protein that belongs to the non-histone chromosomal high mobility group (HMG) family. HMGA1 has been shown to play a role in the regulation of gene transcription by binding to DNA and modifying its structure, thereby influencing the interaction between DNA and other proteins involved in transcription.
The HMGA1 protein exists in several isoforms due to alternative splicing, one of which is HMGA1c. HMGA1c is a splicing variant of HMGA1 that contains an additional 39 amino acids at its C-terminus compared to other isoforms.
It's important to note that there seems to be some confusion in the literature regarding the definition and naming of HMGA1 isoforms, including HMGA1c. Therefore, it's crucial to consider the context and specific nomenclature used in each study when interpreting results related to this protein.
In summary, HMGA1c is a splicing variant of the HMGA1 protein that has an additional 39 amino acids at its C-terminus and plays a role in gene transcription regulation by binding to DNA and modifying its structure.
A lipoma is a common, benign (non-cancerous) soft tissue growth. It is composed of adipose or fatty tissue and typically found just beneath the skin, but they can also occur deeper within the body. Lipomas are usually round, moveable, and painless, although they may cause discomfort if they grow large enough to put pressure on nearby nerves or if they're located in a sensitive area. They generally grow slowly over time. Surgical removal is an option if the lipoma becomes bothersome or grows significantly in size. It's important to note that while lipomas are typically harmless, any new lumps or bumps should be evaluated by a healthcare professional to confirm the diagnosis and rule out other more serious conditions.
Homogentisate 1,2-dioxygenase (HGD) is an enzyme that plays a crucial role in the catabolism of tyrosine, an aromatic amino acid. This enzyme is involved in the third step of the tyrosine degradation pathway, also known as the tyrosine breakdown or catabolic pathway.
The homogentisate 1,2-dioxygenase enzyme catalyzes the conversion of homogentisic acid (HGA) into maleylacetoacetic acid. This reaction involves the cleavage of the aromatic ring of HGA and the introduction of oxygen, hence the name 'dioxygenase.' The reaction can be summarized as follows:
Homogentisate + O2 → Maleylacetoacetate
Deficiency or dysfunction in homogentisate 1,2-dioxygenase leads to a rare genetic disorder called alkaptonuria. In this condition, the body cannot break down tyrosine properly, resulting in an accumulation of HGA and its oxidation product, alkapton, which can cause damage to connective tissues and joints over time.
High Mobility Group Box 3 (HMGB3) protein, also known as HMG-IY, is a member of the high mobility group box (HMGB) family of proteins. These proteins are characterized by their ability to bind to DNA and function as architectural factors in the regulation of gene transcription, DNA replication, and repair.
HMGB3 protein is widely expressed in various tissues, including the testis, brain, heart, lung, liver, skeletal muscle, and kidney. It has been implicated in several biological processes, such as embryonic development, cell differentiation, and tumorigenesis. HMGB3 can act as a transcriptional regulator by binding to specific DNA sequences and interacting with other proteins involved in gene expression.
In cancer, HMGB3 has been found to be overexpressed in several types of malignancies, including hepatocellular carcinoma, colorectal cancer, gastric cancer, and breast cancer. High levels of HMGB3 have been associated with poor prognosis, increased tumor growth, and metastasis. Therefore, HMGB3 is considered a potential therapeutic target for cancer treatment.
MicroRNA
Cancer epigenetics
HMGA1
Santa Ono
List of MeSH codes (D12.776.660)
Origin of replication
List of MeSH codes (D12.776)
Low-frequency variants in HMGA1 are not associated with type 2 diabetes risk
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Romanos Sklavenitis Pistofidis, M.D. | Harvard Catalyst Profiles | Harvard Catalyst
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12q14.3 microdeletion involving HMGA2 gene cause a Silver-Russell syndrome-like phenotype: a case report and review of the...
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HMGA1 protein levels in HPNE-K-RASCHMGA1 (HMGA1) cells set alongside the HPNE-K-RAS-GFP (control) cells and individual...
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SZGR2
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Dynamic interaction of HMGA1a proteins with chromatin | Journal of Cell Science | The Company of Biologists
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HILLION HMGA1B TARGETS
D ornitine decarboxylase (ODC) were included as positive and negative control | Elastase Inhibitor
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SZGR2
NDF-RT Code NDF-RT Name
NEW (2002) MESH HEADINGS WITH SCOPE NOTES (UNIT RECORD FORMAT; 8/27/2001
Chromatin6
- It is the full-length product of the alternatively-spliced HMGA1 gene and may function as an architectural chromatin binding protein that is involved in transcriptional regulation. (nih.gov)
- Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation. (embl.de)
- Chromatin target of Prmt1 (Chtop) is a vertebrate-specific chromatin-bound protein that plays an important role in transcriptional regulation. (embl.de)
- HMGA chromatin binding proteins get excited about diverse biological procedures by virtue of their capability to regulate gene appearance (11C33). (eyesoftheelephants.com)
- Since phosphorylation of HMGA proteins significantly reduces their binding affinity for A/T-rich DNA [109,136], hyper-phosphorylation likely results in partial displacement of HMGA proteins from DNA and the formation of a less condensed chromatin structure that is more easily digested by nucleases. (mg132.com)
- Hypo-phosphorylated HMGA proteins, on the other hand, have an increased overall positive change that facilitates tighter DNA binding, chromatin condensation and placement of HMGA:DNA complexes into apoptotic bodies [41]. (mg132.com)
HMGA Proteins8
- The expression of HMGA proteins is high in early developmental stages in embryos and mesenchymal stem cells, whilst it is almost absent or very low in adult tissues. (biomedcentral.com)
- For example, the early stages of apoptosis are first accompanied by a global hyper-phosphorylation, which is quickly followed by a massive de-phosphorylation, of the total population of cellular HMGA proteins [41]. (mg132.com)
- Other site-specific PTMs of HMGA proteins, such as acetylation of K60 of HMGA1b [50] and methylation of R25 of HMGA1a [146-148], have also been reported to occur during apoptosis but the function(s) of such modifications in the death process is unknown. (mg132.com)
- In contrast to induction of apoptosis in normal cells, overexpression of HMGA proteins in some "pre-disposed" normal cells, as well as in immortalized cell lines that have already breached the senescence barrier, often has anti-apoptotic affects [85-87] and frequently induces overt cancerous transformation [34,72,168,169]. (mg132.com)
- HMGA proteins have recently been directly implicated in the process of senescence, or aging, of normal cells. (mg132.com)
- HMGA Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
- This graph shows the total number of publications written about "HMGA Proteins" by people in this website by year, and whether "HMGA Proteins" was a major or minor topic of these publications. (uchicago.edu)
- Below are the most recent publications written about "HMGA Proteins" by people in Profiles. (uchicago.edu)
HMGA23
- HMGA2 gene encodes for the HMGA2 protein, member of the "high-mobility group AT-hook" (HMGA) family. (biomedcentral.com)
- We lately reported high degrees of (gene encodes the HMGA1a and HMGA1b proteins isoforms that derive from additionally spliced RNA and differ by an interior 11 proteins, present just in the HMGA1a isoform (11C13), while HMGA2 is certainly encoded by another gene (13, 16, 24, 27, 32C33). (eyesoftheelephants.com)
- And, importantly for the present discussion, SAHFs are depleted in linker histone H1 and enriched for HMGA1 and HMGA2, proteins which have been demonstrated to be essential components of these heterochromatin structures [56,107,176]. (mg132.com)
TRANSCRIPTION FACTORS1
- These proteins act as architectural transcription factors that regulate the trascriptional activity of several genes. (biomedcentral.com)
NUCLEOPROTEINS1
- Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. (lookformedical.com)
MOTIFS2
- An 11-kDa AT-hook motif-containing ( AT-HOOK MOTIFS ) protein that binds to the minor grove of AT-rich regions of DNA . (nih.gov)
- Proteins containing AT-HOOK MOTIFS that are rich in arginine and glycine residues. (uchicago.edu)
Substances1
- Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. (lookformedical.com)
Gene5
- miRNAs base-pair to complementary sequences in mRNA molecules, then gene silence said mRNA molecules by one or more of the following processes: Cleavage of mRNA strand into two pieces, Destabilization of mRNA by shortening its poly(A) tail, or Translation of mRNA into proteins. (wikipedia.org)
- Transcriptional regulation of the human ferritin gene by coordinated regulation of Nrf2 and protein arginine methyltransferases PRMT1 and PRMT4. (embl.de)
- Mutations in the gene for the antennapedia homeodomain protein are associated with the conversion of antenna to leg or leg to antenna DROSOPHILA. (lookformedical.com)
- Homeodomain proteins are involved in the control of gene expression during morphogenesis and development (GENE EXPRESSION REGULATION, DEVELOPMENTAL). (lookformedical.com)
- HMGA protein are AT-hook protein that bind towards the minimal groove of DNA at AT wealthy locations (11C13, 33C35), recruit extra transcription elements, and in collaboration with these elements, alter gene appearance (11). (eyesoftheelephants.com)
MRNA3
- isolated the lin-4 miRNA, they found that instead of producing an mRNA encoding a protein, it produced short non-coding RNAs, one of which was a ~22-nucleotide RNA that contained sequences partially complementary to multiple sequences in the 3' UTR of the lin-14 mRNA. (wikipedia.org)
- This complementarity was proposed to inhibit the translation of the lin-14 mRNA into the LIN-14 protein. (wikipedia.org)
- proteins and mRNA had been elevated in the cells transduced using the HMGA1a lentivirus as proven by quantitative, change transcriptase real-time PCR (qRT-PCR) and Traditional western evaluation (Fig. 1A). (eyesoftheelephants.com)
Architectural1
- The assembly of PRMT6 protein network allowed us to formulate functional hypotheses which led to the discovery of new molecular partners for the architectural transcription factor HMGA1a, a known substrate for PRMT6, and to provide evidences for a modulatory role of HMGA1a on the methyltransferase activity of PRMT6. (embl.de)
Methylation3
- To test our hypothesis that histone H4R3 and H3R17 methylation regulates ferritin transcription, H4R3 and H3R17 protein arginine (R) methyltransferases 1 and 4 (PRMT1 and PRMT4) were investigated. (embl.de)
- We describe the residue-specific methylation of E2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetric dimethylating PRMT5 and relate the marks to different functional consequences of E2F-1 activity. (embl.de)
- The Tudor domain protein p100-TSN reads the symmetric methylation mark, and binding of p100-TSN downregulates E2F-1 apoptotic activity. (embl.de)
Condensates1
- In this study, we demonstrate that formation and regulation of PRC1 condensates are consistent with the scaffold-client model, where the Chromobox 2 (CBX2) protein behaves as the scaffold while the other PRC1 proteins are clients. (bvsalud.org)
Arginine2
GENES2
- Proteins encoded by homeobox genes (GENES, HOMEOBOX) that exhibit structural similarity to certain prokaryotic and eukaryotic DNA-binding proteins. (lookformedical.com)
- The proteins encoded by homeobox genes are called HOMEODOMAIN PROTEINS. (lookformedical.com)
Nucleus1
- Proteins found in the nucleus of a cell. (lookformedical.com)
Bind2
- Proteins which bind to DNA. (lookformedical.com)
- The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. (lookformedical.com)
Cellular1
- We propose that sorbitol is a mechanosensitive metabolite enabling protein condensation to control mechano-regulated cellular functions. (bvsalud.org)
Species2
- Proteins that originate from insect species belonging to the genus DROSOPHILA. (lookformedical.com)
- The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development. (lookformedical.com)
Family1
- The Bcl-2 homology 3 (BH3) domain is crucial for the death-inducing and dimerization properties of pro-apoptotic members of the Bcl-2 protein family, including Bak, Bax, and Bad. (lookformedical.com)
Variant1
- SAHFs also contain heterochromatin protein 1 (HP1) and the transcriptionally repressive histone variant macroH2A [56,106,176]. (mg132.com)
Network1
- This network included the abundant pattern recognition proteins, signal transduction compo nents involved with Toll, Imd and JAK/STAT pathways, modulation molecules in proPO activating cascade and immune responsive effectors. (cox2-inhibitors.com)
Control1
- The Traditional western blot displays Pexacerfont the elevated HMGA1 proteins in the HPNE-K-RAS-HMGA1 cells (denoted HMGA1) set alongside the control HPNE-K-RAS cells (denoted control). (eyesoftheelephants.com)
Formation1
- Phase separation plays an important role in the formation of membraneless compartments within the cell and intrinsically disordered proteins with low-complexity sequences can drive this compartmentalisation. (bvsalud.org)
Results1
- PPI (protein-protein interaction) results are shown above. (ihb.ac.cn)
Function1
- Several other genetic backgrounds result in enlargement of the haltere significantly beyond the normal range of haploinsufficient phenotypes, suggesting genetic variation in cofactors that mediate homeotic protein function. (lookformedical.com)