Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

被引：490

作者：

Bochkarev, A ^{[1
]}

Pfuetzner, RA ^{[1
]}

Edwards, AM ^{[1
]}

Frappier, L ^{[1
]}

机构：

[1] MCMASTER UNIV,INST MOL BIOL & BIOTECHNOL,CANC RES GRP,HAMILTON,ON L8N 3Z5,CANADA

来源：

NATURE | 1997年 / 385卷 / 6612期

关键词：

D O I：

10.1038/385176a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

THE single-stranded-DNA-binding proteins (SSBs) are essential fur DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses(1,2). The structures of four SSBs have been solved(3-7), but the molecular details of the interaction of SSBs with DNA remain speculative. We report here the crystal structure at 2.4 Angstrom resolution of the single-stranded-DNA-binding domain of human replication protein A (RPA) bound to DNA. Replication protein a is a heterotrimeric SSB that is highly conserved in eukaryotes. The largest subunit, RPA70, binds to single-stranded (ss)DNA(8,9) and mediates interactions with many cellular and viral proteins(10). The DNA-binding domain, which ties in the middle of RPA70, comprises two structurally homologous subdomains oriented in tandem. The ssDNA lies in a channel that extends from one subdomain lo the other. The structure of each RPA70 subdomain is similar to those of the bacteriophage SSBs, indicating that the mechanism of ssDNA-binding is conserved.

引用

页码：176 / 181

页数：6

共 24 条

[1] CHARACTERIZATION OF DNA-BINDING AND STRAND-EXCHANGE STIMULATION PROPERTIES OF Y-RPA, A YEAST SINGLE-STRAND-DNA-BINDING PROTEIN [J].

ALANI, E ;

THRESHER, R ;

GRIFFITH, JD ;

KOLODNER, RD .

JOURNAL OF MOLECULAR BIOLOGY, 1992, 227 (01) :54-71

[2] OVEREXPRESSION, PURIFICATION, AND CRYSTALLIZATION OF THE DNA-BINDING AND DIMERIZATION DOMAINS OF THE EPSTEIN-BARR-VIRUS NUCLEAR ANTIGEN-1 [J].

BARWELL, JA ;

BOCHKAREV, A ;

PFUETZNER, RA ;

TONG, H ;

YANG, DSC ;

FRAPPIER, L ;

EDWARDS, AM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (35) :20556-20559

[3]

Blackwell LJ, 1996, MOL CELL BIOL, V16, P4798

[4] HUMAN REPLICATION PROTEIN-A BINDS SINGLE-STRANDED-DNA IN 2 DISTINCT COMPLEXES [J].

BLACKWELL, LJ ;

BOROWIEC, JA .

MOLECULAR AND CELLULAR BIOLOGY, 1994, 14 (06) :3993-4001

[5] CRYSTALLOGRAPHIC R-FACTOR REFINEMENT BY MOLECULAR-DYNAMICS [J].

BRUNGER, AT ;

KURIYAN, J ;

KARPLUS, M .

SCIENCE, 1987, 235 (4787) :458-460

[6] ACCURATE BOND AND ANGLE PARAMETERS FOR X-RAY PROTEIN-STRUCTURE REFINEMENT [J].

ENGH, RA ;

HUBER, R .

ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 :392-400

[7] THE SOLUTION STRUCTURE OF THE TYR41-]HIS MUTANT OF THE SINGLE-STRANDED-DNA BINDING-PROTEIN ENCODED BY GENE-V OF THE FILAMENTOUS BACTERIOPHAGE M13 [J].

FOLKERS, PJM ;

NILGES, M ;

FOLMER, RHA ;

KONINGS, RNH ;

HILBERS, CW .

JOURNAL OF MOLECULAR BIOLOGY, 1994, 236 (01) :229-246

[8] SOLUTION STRUCTURE OF THE SINGLE-STRANDED-DNA BINDING-PROTEIN OF THE FILAMENTOUS PSEUDOMONAS PHAGE PF3 - SIMILARITY TO OTHER PROTEINS BINDING TO SINGLE-STRANDED NUCLEIC-ACIDS [J].

FOLMER, RHA ;

NILGES, M ;

KONINGS, RNH ;

HILBERS, CW .

EMBO JOURNAL, 1995, 14 (17) :4132-4142

[9]

FUREY W, IN PRESS METH ENZYMO

[10] Proteolytic mapping of human replication protein A: Evidence for multiple structural domains and a conformational change upon interaction with single-stranded DNA [J].

Gomes, XV ;

Henricksen, LA ;

Wold, MS .

BIOCHEMISTRY, 1996, 35 (17) :5586-5595

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