Single-molecule analysis reveals two distinct states of the compressed RecA filament on single-stranded DNA

被引：4

作者：

Alekseev, Aleksandr ^{[1
]}

Serdakov, Maksim ^{[1
]}

Pobegalov, Georgii ^{[1
]}

Yakimov, Alexandr ^{[1
,2
]}

Bakhlanova, Irina ^{[2
]}

Baitin, Dmitry ^{[2
]}

Khodorkovskii, Mikhail ^{[1
,3
]}

机构：

[1] Peter Great St Petersburg Polytech Univ, St Petersburg 195251, Russia

[2] BP Konstantinov Natl Res Ctr Kurchatov Inst, Dept Mol & Radiat Biophys, Petersburg Nucl Phys Inst, Gatchina, Russia

[3] Russian Acad Sci, Inst Cytol, St Petersburg, Russia

来源：

FEBS LETTERS | 2020年 / 594卷 / 21期

基金：

俄罗斯科学基金会;

关键词：

ATP hydrolysis; homologous recombination; RecA; single-molecule biophysics; PROMOTED ATP HYDROLYSIS; HUMAN RAD51; EXCHANGE-REACTION; HOMOLOGOUS RECOMBINATION; NUCLEOPROTEIN FILAMENT; ESCHERICHIA-COLI; PROTEIN; BINDING; MECHANISM; COMPLEXES;

D O I：

10.1002/1873-3468.13922

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The RecA protein plays a key role in bacterial homologous recombination (HR) and acts through assembly of long helical filaments around single-stranded DNA in the presence of ATP. Large-scale conformational changes induced by ATP hydrolysis result in transitions between stretched and compressed forms of the filament. Here, using a single-molecule approach, we show that compressed RecA nucleoprotein filaments can exist in two distinct interconvertible states depending on the presence of ADP in the monomer-monomer interface. Binding of ADP promotes cooperative conformational transitions and directly affects mechanical properties of the filament. Our findings reveal that RecA nucleoprotein filaments are able to continuously cycle between three mechanically distinct states that might have important implications for RecA-mediated processes of HR.

引用

页码：3464 / 3476

页数：13

共 72 条

[11] Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures [J].

Chen, Zhucheng ;

Yang, Haijuan ;

Pavletich, Nikola P. .

NATURE, 2008, 453 (7194) :489-U3

[12] Organized unidirectional waves of ATP hydrolysis within a RecA filament [J].

Cox, JM ;

Tsodikov, OV ;

Cox, MM .

PLOS BIOLOGY, 2005, 3 (02) :231-243

[13] Regulation of bacterial RecA protein function [J].

Cox, Michael M. .

CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2007, 42 (01) :41-63

[14]

COX MM, 1981, J BIOL CHEM, V256, P4676

[15]

COX MM, 1982, J BIOL CHEM, V257, P8523

[16] ATP hydrolysis provides functions that promote rejection of pairings between different copies of long repeated sequences [J].

Danilowicz, Claudia ;

Hermans, Laura ;

Coljee, Vincent ;

Prevost, Chantal ;

Prentiss, Mara .

NUCLEIC ACIDS RESEARCH, 2017, 45 (14) :8448-8462

[17] RecA and DNA recombination: a review of molecular mechanisms [J].

del Val, Elsa ;

Nasser, William ;

Abaibou, Hafid ;

Reverchon, Sylvie .

BIOCHEMICAL SOCIETY TRANSACTIONS, 2019, 47 :1511-1531

[18] COMPLEXES OF RECA PROTEIN IN SOLUTION - A STUDY BY SMALL-ANGLE NEUTRON-SCATTERING [J].

DICAPUA, E ;

SCHNARR, M ;

RUIGROK, RWH ;

LINDNER, P ;

TIMMINS, PA .

JOURNAL OF MOLECULAR BIOLOGY, 1990, 214 (02) :557-570

[19] A RecA filament capping mechanism for RecX protein [J].

Drees, JC ;

Lusetti, SL ;

Chitteni-Pattu, S ;

Inman, RB ;

Cox, MM .

MOLECULAR CELL, 2004, 15 (05) :789-798

[20] Difference between active and inactive nucleotide cofactors in the effect on the DNA binding and the helical structure of RecA filament -: Dissociation of RecA-DNA complex by inactive nucleotides [J].

Ellouze, C ;

Selmane, T ;

Kim, HK ;

Tuite, E ;

Nordén, B ;

Mortensen, K ;

Takahashi, M .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 262 (01) :88-94

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