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

被引：89

作者：

Huang, Yen-Hua ^{[1
]}

Huang, Cheng-Yang ^{[1
,2
]}

机构：

[1] Chung Shan Med Univ, Sch Biomed Sci, Taichung 40201, Taiwan

[2] Chung Shan Med Univ Hosp, Dept Med Res, Taichung 40201, Taiwan

来源：

BIOMED RESEARCH INTERNATIONAL | 2014年 / 2014卷

关键词：

STALLED REPLICATION FORKS; PHI X174-TYPE PRIMOSOME; N-TERMINAL DOMAIN; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; HEXAMERIC HELICASE; RESTART PRIMOSOME; COMPLEX-FORMATION; LAGGING-STRAND; OB-FOLD;

D O I：

10.1155/2014/195162

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页数：14

共 102 条

[1]

ALLEN GC, 1993, J BIOL CHEM, V268, P19204

[2] UNIQUE PRIMED START OF PHAGE PHI-X174 DNA-REPLICATION AND MOBILITY OF THE PRIMOSOME IN A DIRECTION OPPOSITE CHAIN SYNTHESIS [J].

ARAI, K ;

KORNBERG, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (01) :69-73

[3]

ARAI K, 1981, J BIOL CHEM, V256, P5281

[4] The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling [J].

Arnold, K ;

Bordoli, L ;

Kopp, J ;

Schwede, T .

BIOINFORMATICS, 2006, 22 (02) :195-201

[5] Structural mechanisms of PriA-mediated DNA replication restart [J].

Bhattacharyya, Basudeb ;

George, Nicholas P. ;

Thurmes, Tiffany M. ;

Zhou, Ruobo ;

Jani, Niketa ;

Wessel, Sarah R. ;

Sandler, Steven J. ;

Ha, Taekjip ;

Keck, James L. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (04) :1373-1378

[6] Genes Required for Growth at High Hydrostatic Pressure in Escherichia coli K-12 Identified by Genome-Wide Screening [J].

Black, S. Lucas ;

Dawson, Angela ;

Ward, F. Bruce ;

Allen, Rosalind J. .

PLOS ONE, 2013, 8 (09)

[7] A novel dnaC mutation that suppresses priB rep mutant phenotypes in Escherichia coli K-12 [J].

Boonsombat, R ;

Yeh, SP ;

Milne, A ;

Sandler, SJ .

MOLECULAR MICROBIOLOGY, 2006, 60 (04) :973-983

[8] Bad Bugs, No Drugs: No ESKAPE! An Update from the Infectious Diseases Society of America [J].

Boucher, Helen W. ;

Talbot, George H. ;

Bradley, John S. ;

Edwards, John E., Jr. ;

Gilbert, David ;

Rice, Louis B. ;

Scheld, Michael ;

Spellberg, Brad ;

Bartlett, John .

CLINICAL INFECTIOUS DISEASES, 2009, 48 (01) :1-12

[9] Structural basis for DNA duplex separation by a superfamily-2 helicase [J].

Buettner, Katharina ;

Nehring, Sebastian ;

Hopfner, Karl-Peter .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (07) :647-652

[10] Alarming β-lactamase-mediated resistance in multidrug-resistant Enterobacteriaceae [J].

Bush, Karen .

CURRENT OPINION IN MICROBIOLOGY, 2010, 13 (05) :558-564

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