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Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library
Protein-protein interactions (PPIs) are essential events to play important roles in a series of biological processes. There are probably more ways of PPIs than we currently realized. Structural and functional investigations of weak PPIs have lagged behind those of strong PPIs due to technical diffic...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3913781/ https://www.ncbi.nlm.nih.gov/pubmed/24505465 http://dx.doi.org/10.1371/journal.pone.0088286 |
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author | Mu, Yi Cai, Pengfei Hu, Siqi Ma, Sucan Gao, Youhe |
author_facet | Mu, Yi Cai, Pengfei Hu, Siqi Ma, Sucan Gao, Youhe |
author_sort | Mu, Yi |
collection | PubMed |
description | Protein-protein interactions (PPIs) are essential events to play important roles in a series of biological processes. There are probably more ways of PPIs than we currently realized. Structural and functional investigations of weak PPIs have lagged behind those of strong PPIs due to technical difficulties. Weak PPIs are often short-lived, which may result in more dynamic signals with important biological roles within and/or between cells. For example, the characteristics of PSD-95/Dlg/ZO-1 (PDZ) domain binding to internal sequences, which are primarily weak interactions, have not yet been systematically explored. In the present study, we constructed a nearly random octapeptide yeast two-hybrid library. A total of 24 PDZ domains were used as baits for screening the library. Fourteen of these domains were able to bind internal PDZ-domain binding motifs (PBMs), and PBMs screened for nine PDZ domains exhibited strong preferences. Among 11 PDZ domains that have not been reported their internal PBM binding ability, six were confirmed to bind internal PBMs. The first PDZ domain of LNX2, which has not been reported to bind C-terminal PBMs, was found to bind internal PBMs. These results suggest that the internal PBMs binding ability of PDZ domains may have been underestimated. The data provided diverse internal binding properties for several PDZ domains that may help identify their novel binding partners. |
format | Online Article Text |
id | pubmed-3913781 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39137812014-02-06 Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library Mu, Yi Cai, Pengfei Hu, Siqi Ma, Sucan Gao, Youhe PLoS One Research Article Protein-protein interactions (PPIs) are essential events to play important roles in a series of biological processes. There are probably more ways of PPIs than we currently realized. Structural and functional investigations of weak PPIs have lagged behind those of strong PPIs due to technical difficulties. Weak PPIs are often short-lived, which may result in more dynamic signals with important biological roles within and/or between cells. For example, the characteristics of PSD-95/Dlg/ZO-1 (PDZ) domain binding to internal sequences, which are primarily weak interactions, have not yet been systematically explored. In the present study, we constructed a nearly random octapeptide yeast two-hybrid library. A total of 24 PDZ domains were used as baits for screening the library. Fourteen of these domains were able to bind internal PDZ-domain binding motifs (PBMs), and PBMs screened for nine PDZ domains exhibited strong preferences. Among 11 PDZ domains that have not been reported their internal PBM binding ability, six were confirmed to bind internal PBMs. The first PDZ domain of LNX2, which has not been reported to bind C-terminal PBMs, was found to bind internal PBMs. These results suggest that the internal PBMs binding ability of PDZ domains may have been underestimated. The data provided diverse internal binding properties for several PDZ domains that may help identify their novel binding partners. Public Library of Science 2014-02-04 /pmc/articles/PMC3913781/ /pubmed/24505465 http://dx.doi.org/10.1371/journal.pone.0088286 Text en © 2014 Mu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Mu, Yi Cai, Pengfei Hu, Siqi Ma, Sucan Gao, Youhe Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library |
title | Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library |
title_full | Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library |
title_fullStr | Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library |
title_full_unstemmed | Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library |
title_short | Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library |
title_sort | characterization of diverse internal binding specificities of pdz domains by yeast two-hybrid screening of a special peptide library |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3913781/ https://www.ncbi.nlm.nih.gov/pubmed/24505465 http://dx.doi.org/10.1371/journal.pone.0088286 |
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