We were interested in characterizing proteins involved in telomere-membrane interactions in human sperm. To this end, nuclear membranes were partially solubilized by treatment with 0.5% Triton X-100 in buffer containing 100 mM NaCl. Earlier FISH data (Zalensky et al. 1995) demonstrated that such treatment destroyed association of human sperm telomeres with nuclear membrane. Usual methods for telomere-binding protein isolation involve nuclei extraction with salt buffers of higher molarity (e.g., 0.6 M KCl). Surprisingly, a Triton extract of human sperm was active in binding ds(TTAGGG) DNA, and this telomere-binding activity appeared to be identical to hSTBP previously described in 0.5 M NaCl nuclear extracts (Zalensky et al. 1997) as judged by a characteristic gel-retardation pattern (Fig. 1 a). The pretreatment of crude Triton-soluble hSTBP (hSTBPTR) with 6 M Urea, DNAase, and RNAase does not influence ds(TTAGGG) binding, at the same time activity is sensitive to temperature, and destroyed by ...
The yeast ARS binding factor 1 (ABF1)--where ARS is an autonomously replicating sequence--and repressor/activator protein 1 (RAP1) have been implicated in DNA replication, transcriptional activation, and transcriptional silencing. The ABF1 gene was cloned and sequenced and shown to be essential for viability. The predicted amino acid sequence contains a novel sequence motif related to the zinc finger, and the ABF1 protein requires zinc and unmodified cysteine residues for sequence-specific DNA binding. Interestingly, ABF1 is extensively related to its counterpart, RAP1, and both proteins share a region of similarity with SAN1, a suppressor of certain SIR4 mutations, suggesting that this region may be involved in mediating SIR function at the silent mating type loci.. ...
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We have previously shown, that in plant cells, similarly to human, animal and protozoan cells, telomeres are maintained by telomerase, the specialised ribonucleoprotein complex of reverse-transcriptase activity. Our subsequent studies revealed the con
Telomeres belong to the key functional elements of eukaryotic chromosomes. Like all the other parts of the genome, they exist and function as complexes of DNA with histones and various nonhistone proteins, including specific telomere-binding proteins.
OBFC1, 0.25 mg. CST complex subunit STN1, also known as OBFC1, is a component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation.
Complete information for ACD gene (Protein Coding), ACD, Shelterin Complex Subunit And Telomerase Recruitment Factor, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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It almost sounds like you are trying to ,, replace the principal of having fill-in ,, digis that respond to WIDE1-1 at low ,, elevations and high WIDEn-N digis... , , This idea was born dead. Not so fast. It was the only way in the USA to allow the construction of FILL-IN digis using the hundreds of thousands of existing available TNCs already in hand and not require the use of a $280 specialized new-N APRS TNC. , Our scheme, where everybody uses WIDE2-2, , and fill-in-digis respond only to packets , from a certain geographical region, works far better. Yes, it is slightly better because the length of each packet is shorter without having to carry the initial WIDE1-1. And it is the best solution, if people are willing to buy all-new hardware for fill-in digis. It is good to hear that your country is able to do this. We should be able to slowly migrate that direction now that many innexpensive new-N TNC digipeaters are available. But for years, users will still have to use the path of WIDE1-1 ...
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The CDC13 gene has previously been implicated in the maintenance of telomere integrity in Saccharomyces cerevisiae. With the use of two classes of mutations, here it is shown that CDC13 has two discrete roles at the telomere. The cdc13-2est mutation perturbs a function required in vivo for telomerase regulation but not in vitro for enzyme activity, whereas cdc13-1ts defines a separate essential role at the telomere. In vitro, purified Cdc13p binds to single-strand yeast telomeric DNA. Therefore, Cdc13p is a telomere-binding protein required to protect the telomere and mediate access of telomerase to the chromosomal terminus.. ...
POT1 and TPP1 are part of the shelterin complex and are essential for telomere length regulation and maintenance. Naturally occurring mutations of the telomeric POT1-TPP1 complex are implicated in familial glioma, melanoma and chronic lymphocytic leukaemia. Here we report the atomic structure of the interacting portion of the human telomeric POT1-TPP1 complex and suggest how several of these mutations contribute to malignant cancer. The POT1 C-terminus (POT1C) forms a bilobal structure consisting of an OB-fold and a holiday junction resolvase domain. TPP1 consists of several loops and helices involved in extensive interactions with POT1C. Biochemical data shows that several of the cancer-associated mutations, partially disrupt the POT1-TPP1 complex, which affects its ability to bind telomeric DNA efficiently. A defective POT1-TPP1 complex leads to longer and fragile telomeres, which in turn promotes genomic instability and cancer.. ...
TY - JOUR. T1 - Solution structure of the arabidopsis thaliana telomeric repeat-binding protein DNA binding domain. T2 - A new fold with an additional C-terminal helix. AU - Sue, Shih Che. AU - Hsiao, Hsin Hao. AU - Chung, Ben C.P.. AU - Cheng, Ying Hsien. AU - Hsueh, Kuang Lung. AU - Chen, Chung Mong. AU - Ho, Chia Hsing. AU - Huang, Tai Huang. PY - 2006/2/10. Y1 - 2006/2/10. N2 - The double-stranded telomeric repeat-binding protein (TRP) AtTRP1 is isolated from Arabidopsis thaliana. Using gel retardation assays, we defined the C-terminal 97 amino acid residues, Gln464 to Val560 (AtTRP1464-560), as the minimal structured telomeric repeat-binding domain. This region contains a typical Myb DNA-binding motif and a C-terminal extension of 40 amino acid residues. The monomeric AtTRP1464-560 binds to a 13-mer DNA duplex containing a single repeat of an A. thaliana telomeric DNA sequence (GGTTTAG) in a 1:1 complex, with a KD∼10-6-10-7 M. Nuclear magnetic resonance (NMR) examination revealed that the ...
Telomeres are complex nucleoprotein structures that protect the extremities of linear chromosomes. Telomere replication is a major challenge because many obstacles to the progression of the replication fork are concentrated at the ends of the chromosomes. This is known as the telomere replication problem. In this article, different and new aspects of telomere replication, that can threaten the integrity of telomeres, will be reviewed. In particular, we will focus on the functions of shelterin and the replisome for the preservation of telomere integrity
Yeast telomeric DNA is assembled into a nonnucleosomal chromatin structure known as the telosome, which is thought to influence the transcriptional repression of genes placed in its vicinity, a phenomenon called telomere position effect (TPE). The product of the RAP1 gene, Rap1p, is a component of the telosome. We show that the fraction of cells exhibiting TPE can be substantially reduced by expressing large amounts of a deletion derivative of Rap1p that is unable to bind DNA, called Rap1 delta BBp, or by introducing extra telomeres on a linear plasmid, presumably because both compete in trans with telomeric chromatin for factor(s) important for TPE. This reduction in TPE, observed in three different strains, was demonstrated for two different genes, each assayed at a different telomere. In contrast, the addition of internal tracts of telomeric DNA on a circular plasmid had very little effect on TPE. The product of the SIR3 gene, Sir3p, appears to be limiting for TPE. Overexpression of Sir3p ...
PubMed Central Canada (PMC Canada) provides free access to a stable and permanent online digital archive of full-text, peer-reviewed health and life sciences research publications. It builds on PubMed Central (PMC), the U.S. National Institutes of Health (NIH) free digital archive of biomedical and life sciences journal literature and is a member of the broader PMC International (PMCI) network of e-repositories.
Cdc 13 is a Saccharomyces cerevisiae protein that binds to telomeric single-stranded DNA and regulates telomerase activity. Stn 1 has been shown by two-hybrid analysis to form a physical complex with
ZBTB48 binds through the last of its 11 zinc fingers directly to telomeric DNA (TTAGGG, in red) as well as subtelomeric variant repeats (TTGGG/TCAGGG, grey), which represent the protective caps at the end of chromosomes. In addition, it binds to the promoter sequences (dark blue) of specific target genes including mitochondrial fission process 1, MTFP1. In the absence of ZBTB48 (right panel) telomeres become longer whereas the expression of ZBTB48 target genes is strongly reduced. For instance, ZBTB48 KO (knock-out) cells loose the expression of MTFP1 leading to defects in the mitochondrial network with mitochondria clustering around the nucleus instead of being widely spread throughout the cell.
Figure 3. Mutations in STN1 result in abnormal telomere phenotypes. (A) DNA samples, prepared from PBLs of patient P1, her heterozygous father (F1), and a noncarrier sibling (S1) and patient P2, his heterozygous mother (M2), and two independent control samples (C), were analyzed by in-gel hybridization. Duplicated lanes were electrophoresed in the same gel, and then separated and hybridized to a G-rich or C-rich telomeric probe, as indicated above the panels. After native hybridization to detect single-stranded telomeric DNA (top), the gels were denatured and rehybridized with the same probes to detect the overall duplex telomeric DNA (bottom). Treatment with exonuclease I is indicated above the lanes. (B) Graphic illustration of the mean telomere length for the patients and their family members, calculated based on the following number of independent measurements of four in-gels and two Southern analyses: P1:6, M1:3, F1:3, S1:3, P2:9, M2:3, F2:1, C1:2, and C2:3. (C) Graphic illustration of the ...
El Centro Nacional de Biotecnología es un centro estratégico del Consejo Superior de Investigaciones Científicas con un objetivo mixto académico y de transferencia de tecnología en el área de la Biotecnología.
Using a structure-based approach, several small molecule inhibitors of POT1 have been designed to affect telomere integrity by disrupting the binding interaction of human POT1 with its target DNA sequence thereby driving cancer cells into senescence/apoptosis. Using a range of computational tools, a suitable drug binding pocket in POT1 has been identified and the de novo design of a specific class of POT1 inhibitor was completed. Using this novel scaffold, a small focussed library of hit-like compounds were synthesised and screened in a new POT1 fluorescence polarisation displacement assay developed by scientists at the University of Nottingham. In total, over 90 small molecule inhibitors based on two different scaffolds: pyrido[1,2-a]pyrimidines and sulfathiazoles have been synthesized with some inhibitors effectively decreasing POT1-DNA binding between 10-54% at 100μM ligand concentration. The biological results have established that electron-withdrawing substituents on the pendent phenyl ...
Stable telomeres play a key role to the survival of cancer cells; therefore, different cancer chemotherapeutic approaches have been developed in order to disrupt or destabilise telomeres or telomerase. One of the newest methods is the disruption of vital protein-protein interactions in the telomere, such as that between shelterin components TRF1 and TIN2. The principal aim of this project was to obtain a novel peptide-like molecule, an analogue of a key interacting region of TIN2 that could compete effectively for the binding sites on TRF1 and so lead to the destabilisation of telomere structure. Molecular modelling and simulations were undertaken as the starting point of the project. Structure-based drug design was applied, starting from the available crystal structure data. A library of peptide analogues of the TRF1-binding motif in TIN2 was designed using the MM-GBSA simulation method to predict binding affinities. Then, a number of the peptide analogues were selected from the library for ...
Human protection of telomeres 1 ( POT1) gene is a single stranded telomere binding proteins with a critical role in ensuring chromosome stability. There have been variants of POT1gene, and the...
We studied the expression of four telomere-associated proteins (TRF1, TRF2, POT1, and RAP1 genes) in normal and tumor tissues of lung cancer patients and observed significant down-regulation of TRF1 in tumor samples and no significant difference in expression between tumor and normal tissues for TRF2, POT1, and RAP1 (Table 3). The down-regulation of TRF1 in tumor tissue was consistent when we used GAPDH alone, 18S rRNA alone, β-actin alone (data not shown) or the geometric mean of three genes as internal control. In previous published studies, controversial data were presented for these telomeric genes in cancer. Some studies suggested that TRF1 and TRF2 were down-regulated in tumor tissues (21-26), whereas others showed that TRF1 or TRF2 was up-regulated (27-30). Different tumor type and tumor stage may account for some of these differences. One study showed that tumor stage and telomere length might also influence POT1 expression in cancer (31). Their data indicated that in stage I/II gastric ...
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Please put your name below if youre interested in attending. Cutoff date for deciding the sprint dates is 23rd May 2020, please fill-in your availability for dates in between 1-15 June before deadline. Keep list alphabetically sorted. ...
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How is Purpose Of The Spleen abbreviated? POTS stands for Purpose Of The Spleen. POTS is defined as Purpose Of The Spleen very frequently.
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Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5-TTAGGG-3 repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5-TTAGGG-3 sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B
We have purified a 100 kDa protein, resolved in a Southwestern binding screen of total nuclear proteins from Hela cells with double-stranded human telomeric probe. A polyclonal antiserum raised by this protein recognizes purified nucleolin and stains nucleoli in growing Hela cells. We demonstrate that a truncated form of human nucleolin and a purified deletion derivative of mouse nucleolin bind in vitro to duplex telomeric DNA. This study suggests a new link between telomeres and the nucleolus.. ...
Previous work from the de Lange lab showed that TRF2, a shelterin protein that binds to the duplex part of the telomere, is crucial for telomere protection. Without TRF2, telomeres activate a DNA damage signal and are repaired by the same pathways that act on DNA breaks. TRF2 brings a second shelterin protein, POT1, to the telomeres. Because POT1 binds to single-stranded telomeric DNA present at the very end of the chromosomes, the de Lange lab asked how POT1 contributes to the protection of telomeres.. "We had previously removed TRF2 from mouse cells and seen many dramatic phenotypes," says de Lange, "all of the telomeres ligate together; there is a massive DNA damage response and the cells basically die. We argued that if the function of TRF2 was to bring POT1 to the DNA, then we should observe the same phenotype if we removed POT1.". To determine if this was the case, graduate student Dirk Hockemeyer, the first author of the paper, decided to remove the POT1 gene from mice. Humans have one ...
Telomeres, the complex of repetitive DNA and associated proteins at chromosome ends, are essential for chromosome stability. They prevent chromosome ends from fusing and from being recognized as damaged DNA. The telomeres from several organisms have been shown to be located at the nuclear periphery. Transcriptional repression and heterochromatin formation are other processes intimately associated with telomeres and assigned to functional subdomains within the nucleus (reviewed in Greider, 1996; Cockell and Gasser, 1999). Telomeric DNA generally consists of tandemly repeated, short G‐rich sequences and ends with a 3′ overhang, formed by the degradation of the ultimate primer used for synthesizing the lagging strand during DNA replication (reviewed in de Lange, 1995). It was recently observed that telomeres in mammalian cells, ciliates and trypanosomes end with large T loops (for telomere loops), presumably formed by invasion of the 3′ telomeric overhang into the duplex telomeric repeat ...
1221 Telomeres lie at the end of chromosomes and contain the repeat sequence 5′-TTAGGG-3′. At the very ends of each telomeric DNA there is a single-stranded, 3′ overhang of between 50 and 500 bases in the G-rich strand, the so-called G-tail. The G-tail length and telomere binding proteins are essential for formation of t-loop and chromosome maintenance. Dominant negative telomere binding protein TRF2 induces the dissociation of TRF2 binding from telomeres and the destruction of t-loop accompanied by G-tail shortening. Recently, we have developed G-tail telomere HPA, a new technique to measure telomeric G-tail (Nature Methods, 2005). This method has the advantage of being simple to perform, accurate and highly sensitive for G-tails as short as 20 nucleotides. In addition, this assay is specific and quantitative for G-tails, and can be used for large-scale screening to understand diseases associated with ageing and telomere dysfunction. Using this assay, we have measured G-tail length in ...
Background: Telomere length dysregulation plays a major role in cancer development and aging. Telomeres are maintained by a group of specialized genes known as shelterin and shelterin-associated proteins. In breast cancer lines it has been shown that shelterin proteins are dysregulated thereby affecting the telomere stability and contributing to the neoplastic conversion of the mammary epithelial cells. Interestingly, the regulation of some of the shelterin genes is thought to be controlled epigenetically. Methods and Results: In this study, we set out to measure the effect of increased shelterin gene expression on telomere length in breast cancer cell line 21NT treated with 5-aza-2-deoxycytidine (5-aza-CdR) using known telomere length assays. We measured telomere lengths using: Telomere Restriction Fragment length (TRF), absolute quantitative-PCR and cytogenetic Interphase Quantitative Fluorescent in situ Hybridization (iQ-FISH). We found that non-cytotoxic levels of 5-aza-CdR affect telomere ...
The protective caps on chromosome ends - known as telomeres - consist of DNA and associated proteins that are essential for chromosome integrity. A fundamental part of ensuring proper telomere function is maintaining adequate length of the telomeric DNA tract. Telomeric repeat sequences are synthesized by the telomerase reverse transcriptase, and, as such, telomerase is a central player in the maintenance of steady-state telomere length. Evidence from both yeast and mammals suggests that telomere-associated proteins positively or negatively control access of telomerase to the chromosome terminus. In yeast, positive regulation of telomerase access appears to be achieved through recruitment of the enzyme by the end-binding protein Cdc13p. In contrast, duplex-DNA-binding proteins assembled along the telomeric tract exert a feedback system that negatively modulates telomere length by limiting the action of telomerase. In mammalian cells, and perhaps also in yeast, binding of these proteins probably ...
Higher organisms have linear chromosomes, and DNA polymerases are unable to replicate the ends of these chromosomes. Telomeres, repetitive DNA regions of hexanucleotide repeats, protect chromosomal ends from deterioration during DNA replication. Inhibition of telomere extension leads to short telomeres and premature aging-related diseases, whereas uncontrolled telomere lengthening promotes carcinogenesis. Telomerase (TERT), a reverse transcriptase, forms a complex with an RNA template and cofactors to extend telomeres. The shelterin protein complex then binds the 3 single-stranded end of telomeric DNA, protecting it from DNA damage responses. One protein, SLX4, forms a complex involved in DNA repair that includes proteins recently described in telomere regulation. However, many of the proteins that are known to be associated with telomeres have unknown functions. Research into telomeres often utilizes simpler model organisms, such as yeast, meaning that many mechanistic details have yet to be ...
Author Summary Telomeres are protein-DNA structures that protect the ends of eukaryotic chromosomes. A failure in this protective structure can lead to chromosomal instabilities and contribute to cancer and aging. The protective nature of telomeres relies on complex interactions between repetitive telomeric DNA and associated proteins. One major question is how telomeric proteins, including telomere-associated nucleosomes, are modified in order to achieve this protection. In this study, we have discovered that Arabidopsis telomeric nucleosomes contain a unique mixture of both active and inactive chromatin marks. Additionally, the telomeric DNA itself is modified by methylation of cytosines within the telomeric repeat. Regulation of DNA methylation is achieved by telomeric repeat-containing small RNAs, which are derived from the processing of telomeric transcripts by the RNA-dependent DNA methylation pathway. From these data, we infer that the formation of a proper telomere structure is partly regulated