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Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT

Replication restart primosome is a complex dynamic system that is essential for bacterial survival. This system uses various proteins to reinitiate chromosomal DNA replication to maintain genetic integrity after DNA damage. The replication restart primosome in Escherichia coli is composed of PriA he...

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Detalles Bibliográficos
Autores principales: Huang, Yen-Hua, Huang, Cheng-Yang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4129139/
https://www.ncbi.nlm.nih.gov/pubmed/25136561
http://dx.doi.org/10.1155/2014/195162
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author Huang, Yen-Hua
Huang, Cheng-Yang
author_facet Huang, Yen-Hua
Huang, Cheng-Yang
author_sort Huang, Yen-Hua
collection PubMed
description Replication restart primosome is a complex dynamic system that is essential for bacterial survival. This system uses various proteins to reinitiate chromosomal DNA replication to maintain genetic integrity after DNA damage. The replication restart primosome in Escherichia coli is composed of PriA helicase, PriB, PriC, DnaT, DnaC, DnaB helicase, and DnaG primase. The assembly of the protein complexes within the forked DNA responsible for reloading the replicative DnaB helicase anywhere on the chromosome for genome duplication requires the coordination of transient biomolecular interactions. Over the last decade, investigations on the structure and mechanism of these nucleoproteins have provided considerable insight into primosome assembly. In this review, we summarize and discuss our current knowledge and recent advances on the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
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spelling pubmed-41291392014-08-18 Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT Huang, Yen-Hua Huang, Cheng-Yang Biomed Res Int Review Article Replication restart primosome is a complex dynamic system that is essential for bacterial survival. This system uses various proteins to reinitiate chromosomal DNA replication to maintain genetic integrity after DNA damage. The replication restart primosome in Escherichia coli is composed of PriA helicase, PriB, PriC, DnaT, DnaC, DnaB helicase, and DnaG primase. The assembly of the protein complexes within the forked DNA responsible for reloading the replicative DnaB helicase anywhere on the chromosome for genome duplication requires the coordination of transient biomolecular interactions. Over the last decade, investigations on the structure and mechanism of these nucleoproteins have provided considerable insight into primosome assembly. In this review, we summarize and discuss our current knowledge and recent advances on the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT. Hindawi Publishing Corporation 2014 2014-07-21 /pmc/articles/PMC4129139/ /pubmed/25136561 http://dx.doi.org/10.1155/2014/195162 Text en Copyright © 2014 Y.-H. Huang and C.-Y. Huang. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Huang, Yen-Hua
Huang, Cheng-Yang
Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
title Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
title_full Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
title_fullStr Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
title_full_unstemmed Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
title_short Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
title_sort structural insight into the dna-binding mode of the primosomal proteins pria, prib, and dnat
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4129139/
https://www.ncbi.nlm.nih.gov/pubmed/25136561
http://dx.doi.org/10.1155/2014/195162
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