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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...

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Autores principales: 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
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
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.
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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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