In recent years, substantial progress has been made in the identification of proteins involved in peroxisome biogenesis. However, with the exception of the peroxisome-targeting signal receptors and the receptor docking proteins, the function of most of these proteins, called peroxins, remains largely unknown. One step toward elucidating the function of a protein is to identify its interacting partners. We have used a non-transcription-based bacterial two-hybrid system to analyze the interactions among a set of 12 mammalian peroxins and a yeast protein three-hybrid system to investigate whether proteins that interact with the same peroxin and have overlapping binding sites cooperate or compete for this site. Here we report a detailed interaction map of these peroxins and demonstrate that (i) farnesylation, and not the CAAX motif, of Pex19p strongly enhances its affinity for Pex13p; (ii) the CAAXmotif, and not farnesylation, of Pex19p strongly enhances its affinity for Pex11pβ; and (iii) the ...
Matchmaker Monoclonal Antibodies bind specifically to the major activation domain (AD) of yeast two-hybrid prey proteins, or the DNA-binding domain (DNA-BD) of the bait protein.
Matchmaker Monoclonal Antibodies bind specifically to the major activation domain (AD) of yeast two-hybrid prey proteins, or the DNA-binding domain (DNA-BD) of the bait protein.
To capture the Myo1p-interacting proteins for in vitro validation of the physical interactions identified by iMYTH, and for their subsequent identification by coimmunoprecipitation (coIP), we employed a modified pull-down approach (Babu et al. 2009) using a TAP epitope fused to the Myo1p C-terminus (Myo1-TAP). The Myo1-TAP bait strain was transformed with a full-length prey protein in expression vector BG1805, a URA3 multicopy 2 μ plasmid containing a GAL1 promoter (Gelperin et al. 2005), using the standard lithium acetate procedure (Gietz and Woods 2006). The Myo1 protein was captured using the calmodulin-binding peptide in the TAP epitope. Briefly, 40 ml of culture was grown for 2 d in YPD at 30° at 200 rpm. Subsequently, the cells were centrifuged at 3000 rpm for 3 min, and washed twice with 20 ml IPLB buffer (20 mM Hepes KOH, pH 7.4, 150 mM KOAc, 2 mM Mg(Ac)2, 2 mM CaCl2, and 10% glycerol). For plasmid expression, cells were resuspended in YP-GAL, and incubated for 2-4 hr. The yeast cells ...
Easy two-hybrid library construction enriched for longer inserts. Two highly specialized yeast strains that are optimized for exceptionally stringent two-hybrid library screening and two-hybrid library construction.
Four proteins namely U2AF35, SRp40, mDomino and Ddx1 were identified as PHF5a interacting partners by using the murine 11.5-days embryo yeast two-hybrid library screening.PHF5a interacting domains of SR proteins U2AF35 and SRp40 were restricted to Cterminal arginine-serine rich domains (RS).Other members of the SR protein family namely SRp20, SRp30c and ASF/SF2 were shown that they can not bind to the PHF5a protein by using a directed yeast twohybrid assay and the a-galactosidase assay.Protein interactions between PHF5a and U2AF35, SRp40, mDomino and Ddx1 were verified by using in vitro coimmmunoprecipitation assays.Mapping of binding sites by using coimmunoprecipitation experiments and a directed yeast two-hybrid assay demonstrated that both ATP-dependent helicases mDomino and Ddx1 interact with the C-terminal segment of PHF5a. In addition, the N-terminal part of PHF5a was identified as a region responsible for binding to splicing proteins U2AF35 and SRp40. By using the yeast-three hybrid assay ...
proteins function in similar ways. AGS1 binds to the Gβ1 subunit of heterotrimeric G proteins and we have used yeast two-hybrid studies to show that Rhes binds selectively to Gβ1, Gβ2 and Gβ3 subunits. Binding to the Gβ subunits involves the cationic regions of AGS1 and Rhes, and we used Rhes-AGS1 chimeras to show that their different cationic regions determine the Gβ-specificity of the interactions. Possible implications of this interaction for the activity of Rhes are discussed.. ...
If you are regularly doing ChIP-qPCR, ChIP-RNAseq or luciferase reporter assays to measure protein-DNA interactions, then this article is for you! ChIP
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Alternative splicing of precursor mRNA is a fundamental mechanism to generate multiple proteins from a single gene. Although constitutive and alternative mRNA splicing is temporally and spatially regulated, deregulation of mRNA splicing could cause development, progression, and metastasis of tumors. Through yeast two-hybrid screening of a human breast cDNA library using estrogen receptor- (ER) as bait, we identified a novel nuclear receptor box containing full-length protein, nuclear protein E3-3 (NPE3-3). Our results revealed that NPE3-3 associates with not only ER but also with splicing factors, serine/arginine-rich protein (SRp)-30c, SRp40, and splicing factor SC-35, suggesting that NPE3-3 is likely to be involved in regulation of mRNA splicing. Accordingly, transient expression of NPE3-3 in cells resulted in expected splicing of the CD44 control minigene. We also discovered that NPE3-3-overexpressing clones produced a novel, previously unrecognized, alternatively spliced variant of ER ...
Dear colleagues, We are maintaining a Web page devoted to the yeast two-hybrid system. An integral part of this page is a database of false positives, isolated in two-hybrid screenings. We are also trying to analyze the parameters of YTH screens to suggest the optimal settings. We are asking for a favor: if you completed a YTH screen (does not matter if it was a success or a failure), please fill out our questionnaire on the Web page. It is our sincere hope that analysis of these data will be helpful for the scientific community. Our Web page also contains a lot of YTH-related information: list of plasmids, libraries, maps, sequences, protocols etc. http://www.fccc.edu/research/labs/golemis/InteractionTrapInWork.html Best regards, Ilya Serebriiskii ______________O_________oO_____________oO______o_______oO___________________ YEAST bionet newsgroup see: http://www.bio.net/hypermail/YEAST/ YEAST e-mail: messages sent to yeast at net.bio.net subscribe: e-mail biosci-server at net.bio.net with: ...
Activation of PXR by Tian Xian in Cell-Based Assays. To determine the extent to which the extract of tian xian activated human PXR we used a previously described cell-based reporter gene assay (Brobst et al., 2004). In CV-1 cells, 10 μM rifampicin activated the XREM-LUC reporter gene in the presence of transfected human PXR (Fig. 1). A stock extract of tian xian (250 mg/ml) was used to treat transfected CV-1 cells. A clear concentration response was also observed with increasing amounts of tian xian extract (Fig. 1). Thus, in CV-1 cells an extract of tian xian produced efficacious activation of human PXR. The activation of PXR by tian xian at the highest concentrations examined was comparable with that of 10 μM rifampicin, a well known PXR ligand.. Modulation of PXR-Cofactor Interactions in the Mammalian Two-Hybrid System. The interaction between accessory protein cofactors and PXR is modulated by the presence of activating ligands in cells. Specifically, in the absence of activating ligands ...
The fluorescent two-hybrid assay (F2H) is a technique for the validation and characterization of protein-protein interactions in vivo. It can be used for studying the modulation of interactions with inhibitors or activators, for compound screening and for confirmation of results from other protein-protein interaction screens such as co-immunoprecipitation studies.. In short, two proteins, bait and prey protein, are fused to GFP and RFP, respectively. A BHK cell line is transformed with ChromoTeks F2H platform reagent and two DNA plasmids coding for the GFP-bait protein and the RFP-prey protein. The interaction of bait protein and prey protein can be detected by co-localization of a green and a red fluorescent spot in the nucleus of the BHK cells with an epi-fluorescence microscope.. PRODUCTS ...
OUTLINE: Using molecular laboratory techniques, this study examines the biochemical mechanisms by which LZAP activates transcriptional, tumor suppressive activity (both p53-dependent and p53-independent) of ARF and inhibits transcriptional, tumorigenic activity of NF-kB. LZAP regulation of newly identified ARF activities, such as S-phase delay and ARF-mediated B23 degradation are also evaluated. LZAPs tumor suppressive activity is assessed in vivo using a conditional knockout vector to target LZAP in mice and to observe for spontaneous and induced tumor formation. Laboratory analyses used to determine study endpoints include standard recombinant DNA, recombinant protein expression and purification, cell culture and transfection, cell labeling, reporter assays, flow cytometry, yeast-two hybrid, immunoprecipitation, immunoblotting, immunofluorescence, TUNEL assay, ELISA assay, Southern blotting, and protein and gene expression. ...
I have a protein-protein interaction that I have originally detected in bacterial two-hybrid system and pull-down experiments with bacterially expressed proteins also show positive interaction. Now I would like to confirm this interaction also in eukaryotic cells by coimmunoprecipitating the two. Since I do not have antibodies for these proteins, I am using GFP -(Bait) and HA-tagged (target) proteins and thus transfected cells. I have performed the experiment couple of times, and it kind of looks promising: I have positive interaction when the two proteins are present and all negative controls are negative. What makes me doubt is that I do not concentrate the target protein in the immunoprecipitation, that is that my band is weaker in the immunoprecipitation sample than in the original cell lysate sample. In order to have positive interaction do I have to be able to concentrate the target protein? So, what do you think, are these two proteins interacting ...
MdLBD11 interacts with AtAS1 in a yeast two-hybrid assay.Yeast strains containing pGAD-AtAS1, pGBD-MdLBD11, and pGBD-AtAS2 were assayed for LacZ expression, pGA
Two DNA fragments, each encoding the intracellular epitope of rat MuSK [GenBank accession number (Acc. No.) U34985], were linked (named MuSK2xwt) as described before (Cheusova et al., 2006b). The same strategy was applied for the generation of two intracellular domains from a MuSK kinase defective mutant (named MuSK2xkd). MuSK2xwt and MuSK2xkd were subcloned either in pGBKT7 (BD Biosciences Clontech) to generate yeast two-hybrid bait plasmids, or in pCMV5 containing a T7- or a myc-tag to allow expression in mammalian cells. A prey plasmid (pGAD-GH) containing a C-terminal part of human Erbin (GenBank Acc. No. NM_018695.2; starting at position 3017 of the open reading frame and coding for 365 aa) fused in frame to the Gal4 activation domain was identified by yeast two-hybrid. A human HeLa S3 Matchmaker cDNA library (BD Biosciences Clontech) was used for the screen. In total 8.5 × 106 independent yeast clones were screened. Yeast two-hybrid analysis was performed as described previously (Cheusova ...
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Hi all, I have a question regarding the expression level of the bait protein vs the expression of target protein. As a bait vector I use the pAS-2 or a derivate in which expression of the GAL4 fusion protein is driven by the native ADH1 promotor which results in rather high expression. The AD-library was inserted into pAD-GAL4 (Stratagene) where expression of the fusion protein is driven by a truncated form of the ADH1 promoter which results in low expression (not detectable in western). The Stratagene manual says about that:Overexpression of the bait protein can result in a phenomenon called squelching. When squelching occurs, ecxess unbound bait protein (not bound to GAL4 UAS) binds target proteins thereby preventing the target proteins from interacting with the bait proteins, which are bound the UAS. Consequently, transcription of reporter genes is not activated and interacting proteins are not detected. What do you think about this? Shouldnt I combine those two plasmids with different ...
Yeast Two Hybrid system - posted in Molecular Biology: Good morning everyone !! To study the interaction between two bacterial proteins, I´m actually doing (or should I say I´m trying to do ) yeast two hybrid assays. This technique is not used in my lab (at least, not from a long time), so no one can advise me . So, I need your help, to know if some one of you have already had the opportunity to do Y2H assays, so he can may be have the extreme kidness to give me a protocol that...
Yeast two-hybrid results using PKP3 and fragments thereof as baits. Two colonies are shown for each cotransformation, including negative controls. SD-LWHA is th
High-resolution computational models of genome binding events. A bacterial one-hybrid system for determining the DNA-binding specificity of transcription factors
B) to (D) Yeast two-hybrid analysis of interactions between the full-length PKS5 protein (PKS5) or the N- (PKS5N) or C- (PKS5C) terminal portions of theprotein with J3, or J3C-219, J3C1, or J3C2. Interactions between the full-length PKS5 protein or the protein with the FISL domain deleted (PKS5DF) and J3 Activates Plasma Membrane H+-ATPase Activity C-terminal region of the protein (Palmgren et al., 1991). Phos- evolution and is important for protein translation, folding, unfold- phorylation of this C-terminal autoinhibitory domain at the pen- ing, translocation, and degradation in a broad array of cellular ultimate residue (Thr-947) leads to its interaction with a 14-3-3 processes (Boston et al., 1996; Waters et al., 1996; Wang et al., regulatory protein and activation of the H+-ATPase (Svennelid 2004). Expression of Hsps in planta is induced by high temper- et al., 1999; Camoni et al., 2000; Gevaudant et al., 2007). The ature and also by a wide range of other environmental stresses, activated ...
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Molecular Cloning, also known as Maniatis, has served as the foundation of technical expertise in labs worldwide for 30 years. No other manual has been so popular, or so influential.
Aronheim A, et al. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol. Cell. Biol. 17: 3094-3102, 1997. PubMed: 9154808 Brachmann RK, Boeke JD. Tag games in yeast: the two-hybrid system and beyond. Curr. Opin. Biotechnol 8: 561-568, 1997. PubMed: 9353226 ...
Aronheim A, et al. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol. Cell. Biol. 17: 3094-3102, 1997. PubMed: 9154808 Brachmann RK, Boeke JD. Tag games in yeast: the two-hybrid system and beyond. Curr. Opin. Biotechnol 8: 561-568, 1997. PubMed: 9353226 ...
You have performed yeast two hybrid assay to identify proteins that interact with superman and identified a gene coding for kryptonite that interacts with superman. What experiments you will perform to demonstrate that the superman interacts with kryptonite in-vivo (inside nucleus in the cell ...
Co-inmunoprecipitación (CoIP) y ensayos de pull-down son métodos de cerca relacionados para identificar las interacciones proteína-proteína estable. Estos...
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RNA-protein interactions are pivotal in fundamental cellular processes such as translation, mRNA processing, early development, and infection by RNA viruses. However, in spite of the central importance of these interactions, few approaches are available to analyze them rapidly in vivo. We describe a yeast genetic method to detect and analyze RNA-protein interactions in which the binding of a bifunctional RNA to each of two hybrid proteins activates transcription of a reporter gene in vivo. We demonstrate that this three-hybrid system enables the rapid, phenotypic detection of specific RNA-protein interactions. As examples, we use the binding of the iron regulatory protein 1 (IRP1) to the iron response element (IRE), and of HIV trans-activator protein (Tat) to the HIV trans-activation response element (TAR) RNA sequence. The three-hybrid assay we describe relies only on the physical properties of the RNA and protein, and not on their natural biological activities; as a result, it may have broad ...
The S. cerevisiae membrane protein Jen1 is a monocarboxylate-proton symporter which after the addition of glucose to lactic acid-grown cells triggers loss of Jen1p activity and repression of JEN1 gene expression (Paiva et al., 2002; Andrade et al., 2001). This downregulation of the permease is dependent on phosphorylation and ubiquitylation mechanisms, both of which are dependent on proteins interacting with the Jen1p. To identify the proteins involved in this process we developed a system combined structure prediction and the yeast two-hybrid system to overcome the difficulties associated to measuring protein interactions with membrane proteins. Measuring protein interactions between membrane proteins or between membrane proteins and other proteins has proved to be very difficult. The commonly used yeast two-hybrid systems are inefficient for membrane proteins since the interaction must take place in the cell nucleus between soluble proteins. An advantage of the strategy used in our approach is ...
HIV-1 tat, a strong transactivator, is essential for the HIV-1 replication and AIDS progression. The Tat function is markedly inhibited by human anti-oncogene p53. This work was initiated to identify the p53-associated inhibitory mechanism on tat-mediated transactivation. Inhibitory function of P53 was confirmed by co-transfection of tat-expressing Jurkat cells with LTR-CAT plasmid, or H3Tl cells (LTR-CAT integrated HeLa cells) with different ratio of pSV-tat/pCDNA-p53 plasmids. Results from the direct protein-protein .interaction between soluble p53 and tat, and yeast two-hybrid experiments showed that the co-suppression mechanism is unlikely to be due to the direct interaction. CAT activity was not affected by tat in Jurkat cells which were transfected with p53-promoter-CAT or p53-enhancer-CAT, suggesting that the tat-mediated p53 suppression is not directly associated with p53-promoter. Finally, we have tested protein kinase activity in p53-tranfected Jurkat cells, which might phosphorylate ...
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In several cases, the homologous WDR proteins are highly conserved throughout the length of the proteins, and appear to operate in highly analogous mechanisms, with specificity in function conferred by changes in upstream signaling pathways and/or downstream effectors. One case is AGB1, the only clear Arabidopsis ortholog of Gβ [31] (Fig. 1). Loss of AGB1 function leads to developmental pleiotropy including shortened fruits [32] and changes in patterns of cell division in the hypocotyl and root [33]. These phenotypes are associated with the derepression of genes that are normally turned on by auxin, suggesting a role for AGB1 as a negative regulator of auxin signaling [33]. There appears to be one Gα-like protein (GPA1) and two Gγ-like proteins (AGG1 and AGG2) in the Arabidopsis proteome [31], and molecular modeling and yeast two-hybrid studies of potential interactions among AGB1, GPA1 and AGG1 are not inconsistent with the possibility that these could form a heterotrimeric protein [33, 34]. ...
BioAssay record AID 747467 submitted by ChEMBL: Agonist activity at human estrogen receptor-beta by yeast two-hybrid assay in presence of SRC1.
Purpose: : To search for proteins that bind to the Usher syndrome type 3 protein Clarin-1. Methods: : Yeast two-hybrid screening (Fields method) was performed using three baits representing the two predicted extra-cellular loops and the intracellular C-terminal region of the mouse Clarin-1 protein. The expression of recombinant GAL4-baits was confirmed by Western blot analysis. Suitability of the baits for screening was additionally confirmed by transactivation activity tests. Each of the baits was used to screen approximately 1.5 million mouse brain cDNAs for interaction. Isolated positive clones were identified by DNA sequencing and database searching. Potential interaction partners of Clarin-1 were subjected to the mating assay. Results: : Screening the mouse cDNA library with three GAL4-Clarin-1 baits identified 125 positive clones that potentially bind to Clarin-1. 110 of the clones were sequenced, of which 41 were in the correct reading frame with GAL4. Most of those 41 clones were ...
Fingerprint Dive into the research topics of Protocols for screening for binding partners of CCN proteins: Yeast two-hybrid system. Together they form a unique fingerprint. ...
Lehner B، Semple JI، Brown SE، وآخرون. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153-67. PMID 14667819. doi:10.1016/S0888-7543(03)00235-0. ...
TY - JOUR. T1 - RhoB induces apoptosis via direct interaction with TNFAIP1 in HeLa cells. AU - Kim, Dong Myung. AU - Chung, Kyung Sook. AU - Choi, Shin Jung. AU - Jung, Yu Jin. AU - Park, Song Kyu. AU - Han, Gyoon Hee. AU - Ha, Jae Seok. AU - Song, Kyung Bin. AU - Choi, Nam Song. AU - Kim, Hwan Mook. AU - Won, Misun. AU - Seo, Yeon Soo. PY - 2009/12/1. Y1 - 2009/12/1. N2 - RhoB, a tumor suppressor, has emerged as an interesting cancer target, and extensive studies aimed at understanding its role in apoptosis have been performed. In our study, we investigated the involvement of RhoB-interacting molecules in apoptosis. To identify RhoB-interacting proteins, we performed yeast-two hybrid screening assays using RhoB as a bait and isolated TNFAIP1, a TNFα-induced protein containing the BTB/POZ domain. The interaction between RhoB and TNFAIP1 was demonstrated in vivo through coimmunoprecipitation studies and in vitro binding assays. RFP-TNFAIP1 was found to be partially colocalized with EGFP-RhoB. ...
Yeast two-hybrid analysis. The two-hybrid assay was performed as described previously (Kim et al., 1995). The last 7 aa residues (amino acids 1144-1150; AGRETTV) of KIF1Bα in pBHA bait vector were used in the screen. For the yeast two-hybrid assay against various PDZ domains, wild-type and mutant (the last amino acid V to A) KIF1Bα (amino acids 1083-1150) in pBHA were used. The PDZ domains in pGAD10 are as follows: PDZ1 (amino acids 203-327), PDZ2 (304-425), and PDZ3 (454-553) of SAP97; PDZ0 (16-103), PDZ1 (424-505), PDZ2 (607-683), PDZ3 (777-863), PDZ4 (919-1023), and PDZ5 (1139-1224) of S-SCAM; Shank1 PDZ (585-691); PDZ1-2 (51-245) and PDZ2-3 (148-339) of glutamate receptor-interacting protein-2 (GRIP2) and PDZ1 (13-106) and PDZ2 (142-249) of Na+/H+exchanger regulatory factor-1 (NHERF1). The pGAD10 constructs containing the PDZ domains of PSD-95 have been described previously (Kim et al., 1995).. Antibodies. Anti-peptide KIF1Bα antibodies were raised against the following synthetic ...
The pFN11A (BIND) Flexi® Vector is a component of the CheckMate™/Flexi® Vector Mammalian Two-Hybrid System. This ampicillin-resistant vector is designed to express a fusion protein comprised of a DNA-binding domain of the yeast GAL4 gene, a linker segment and an in-frame protein-coding sequence, under the control of the human cytomegalovirus (CMV) immediate early promoter. The pFN11A (BIND) Flexi® Vector encodes a |em>Renilla|/em> luciferase gene which may be used to normalize for transfection differences between samples within an experiment.
Figure 6. ERF17 regulates Chl degradation-related genes. A, Yeast one-hybrid assay showing the activity of LacZ reporters driven by the PPH and NYC promoters and activated by activation domain (AD) fusion with ERF17-8S and ERF17-3S (blue color). The empty vectors pB42AD and pLacZi were used as negative controls (white color). BD, Binding domain. B, Gel-shift analysis of ERF17-8S and ERF17-3S binding to the promoters of PPH and NYC. EMSAs of a GST-labeled probe with ERF17-8S and ERF17-3S proteins are shown. DNA probes represent the promoters of PPH and NYC (probe sequences are shown in Supplemental Table S3). Protein/DNA complexes are indicated by arrows. C, SPR binding profiles of ERF17-8S and ERF17-3S proteins to the promoters of PPH and NYC. Protein concentrations were 275 nm in all lines but the bottom line, for which it was 17.2 nm. RU, Response units. ...
Shop FERM and PDZ domain-containing protein ELISA Kit, Recombinant Protein and FERM and PDZ domain-containing protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
All of the non-structural proteins of poliovirus, including their processing precursors, are involved in the replication of the viral RNA genome. These proteins assemble into a replication complex, which also contains the viral RNA and cellular factors. An understanding of how these viral proteins interact with each other would enhance our understanding of the molecular events occurring during poliovirus infection of the cell. Previously, we have employed the yeast two-hybrid system to construct two separate linkage maps for the polioviral P2 and P3 proteins, respectively. In the present study, we have searched for interacting pairs between the P2 and P3 proteins in a similar inducible yeast two-hybrid system. Although, the primary functions of the proteolytic products of the P2 and P3 domains of the polyprotein in the viral life cycle are different, we observed significant interactions between 2CATPase and 3AB; 2Apro and 3A, 3Cpro or 3Dpol; 2B and 3A or 3AB. All of the interactions were measured in the
In this report, we provide several lines of evidence that p130Cas is a downstream mediator of FAK-promoted cell migration. First, a mutation of P712/715A in FAK abolished its ability to promote CHO cell migration (Fig. 3). The proline-rich region on FAK spanning amino acids 712-718 has been mapped as the primary binding site for p130Cas through its SH3 domain (Polte and Hanks, 1995; Harte et al., 1996), although a second proline-rich region (amino acids 875-884) can also mediate FAK binding to p130Cas (Harte et al., 1996; Polte and Hanks, 1997). In vivo coimmunoprecipitation experiments showed that FAK/ p130Cas association was reduced but not abolished by the P712/715A mutation (Fig. 6), indicating that the second proline-rich region on FAK may mediate some binding to p130Cas, as demonstrated previously (Harte et al., 1996; Polte and Hanks, 1997). However, binding of p130Cas to an alternative site clearly does not allow for FAK-promoted migration. It has also been suggested that p130Cas may ...
Yeast Two Hybrid system uses a reporter gene to detect the interaction of pair of proteins inside the yeast cell nucleus. In the yeast Two Hybrid System, The interaction of target protein to the protein will bring together transcriptional activator, which then switches on the expression of reporter gene.
This article discusses the pull-down technique, which is an invaluable tool for scientists interested in studying cellular pathways via protein-protein interactions.
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At Euromedex we constantly collaborate with french leading researchers to bring new life science products to the scientific community. Therefore we can propose worldwide. -Bacth kit ref EUK001 developed by Mr Ladant (Institut Pasteur). Euromedex bacterial two-hybrid (BACTH, for "Bacterial Adenylate Cyclase-based Two-Hybrid") system is a simple and fast approach to detect and characterize protein-protein interactions in vivo.. -Monoclonals Antibodies for studies of genetic diseases and Transcription Factors (developed by IGBMC - Strasbourg).. EUROMEDEX is continuously looking for high quality products to expand its product portfolio. Please contact us when you are searching for partners to sell you products to the bioscience research community. ...