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The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding
RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped mo...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1885664/ https://www.ncbi.nlm.nih.gov/pubmed/17426134 http://dx.doi.org/10.1093/nar/gkm144 |
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author | Ha, Jun Yong Kim, Hye Kyong Kim, Do Jin Kim, Kyoung Hoon Oh, Sung Jin Lee, Hyung Ho Yoon, Hye Jin Song, Hyun Kyu Suh, Se Won |
author_facet | Ha, Jun Yong Kim, Hye Kyong Kim, Do Jin Kim, Kyoung Hoon Oh, Sung Jin Lee, Hyung Ho Yoon, Hye Jin Song, Hyun Kyu Suh, Se Won |
author_sort | Ha, Jun Yong |
collection | PubMed |
description | RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface (‘interface A’) between tip/center domains is more nonpolar than the other (‘interface B’) between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of ∼30 Å diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination. |
format | Text |
id | pubmed-1885664 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-18856642007-06-07 The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding Ha, Jun Yong Kim, Hye Kyong Kim, Do Jin Kim, Kyoung Hoon Oh, Sung Jin Lee, Hyung Ho Yoon, Hye Jin Song, Hyun Kyu Suh, Se Won Nucleic Acids Res Structural Biology RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface (‘interface A’) between tip/center domains is more nonpolar than the other (‘interface B’) between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of ∼30 Å diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination. Oxford University Press 2007-04 2007-04-10 /pmc/articles/PMC1885664/ /pubmed/17426134 http://dx.doi.org/10.1093/nar/gkm144 Text en © 2007 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Structural Biology Ha, Jun Yong Kim, Hye Kyong Kim, Do Jin Kim, Kyoung Hoon Oh, Sung Jin Lee, Hyung Ho Yoon, Hye Jin Song, Hyun Kyu Suh, Se Won The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding |
title | The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding |
title_full | The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding |
title_fullStr | The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding |
title_full_unstemmed | The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding |
title_short | The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding |
title_sort | recombination-associated protein rdgc adopts a novel toroidal architecture for dna binding |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1885664/ https://www.ncbi.nlm.nih.gov/pubmed/17426134 http://dx.doi.org/10.1093/nar/gkm144 |
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