ATP-mediated changes in cross-subunit interactions in the RecA protein

被引：15

作者：

Logan, KM ^{[1
]}

Forget, AL ^{[1
]}

Verderese, JP ^{[1
]}

Knight, KL ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Dept Mol Pharmacol & Biochem, Worcester, MA 01655 USA

来源：

BIOCHEMISTRY | 2001年 / 40卷 / 38期

关键词：

D O I：

10.1021/bi011081u

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：

RecA protein undergoes ATP- and DNA-induced conformational changes that result in different helical parameters for free protein filaments versus RccA/ATP/DNA nucleoprotein filaments. Previous mutational studies of a particular region of the RecA oligomeric interface suggested that cross-subunit contacts made by residues K6 and R28 were more important for stabilization of free protein oligomers than nucleoprotein filaments [Eldin, S., et al. (2000) J. Mol. Biol. 299, 91 - 101]. Using mutant proteins with specifically engineered Cys substitutions, we show here that the efficiency of cross-subunit disulfide bond formation at certain positions in this region changes in the presence of ATP or ATP/DNA. Our results support the idea that specific cross-subunit interactions that occur within this region of the subunit interface are different in free RecA protein versus RecA/ATP/DNA nucleoprotein filaments.

引用

页码：11382 / 11389

页数：8

共 34 条

[1]

Bianco P. R., 1998, FRONT BIOSCI, V3, pD570, DOI DOI 10.2741/A304

[2] RECA PROTEIN SELF-ASSEMBLY - MULTIPLE DISCRETE AGGREGATION STATES [J].

BRENNER, SL ;

ZLOTNICK, A ;

GRIFFITH, JD .

JOURNAL OF MOLECULAR BIOLOGY, 1988, 204 (04) :959-972

[3] Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament [J].

De Zutter, JK ;

Forget, AL ;

Logan, KM ;

Knight, KL .

STRUCTURE, 2001, 9 (01) :47-55

[4] The hRad51 and RecA proteins show significant differences in cooperative binding to single-stranded DNA [J].

De Zutter, SK ;

Knight, KL .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 293 (04) :769-780

[5] CHARACTERIZATION OF COMPLEXES BETWEEN RECA PROTEIN AND DUPLEX DNA BY ELECTRON-MICROSCOPY [J].

DICAPUA, E ;

ENGEL, A ;

STASIAK, A ;

KOLLER, T .

JOURNAL OF MOLECULAR BIOLOGY, 1982, 157 (01) :87-103

[6] WHAT DO X-RAY CRYSTALLOGRAPHIC AND ELECTRON-MICROSCOPIC STRUCTURAL STUDIES OF THE RECA PROTEIN TELL US ABOUT RECOMBINATION [J].

EGELMAN, EH .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1993, 3 (02) :189-197

[7] STRUCTURE OF HELICAL RECA-DNA COMPLEXES .2. LOCAL CONFORMATIONAL-CHANGES VISUALIZED IN BUNDLES OF RECA-ATP-GAMMA-S FILAMENTS [J].

EGELMAN, EH ;

STASIAK, A .

JOURNAL OF MOLECULAR BIOLOGY, 1988, 200 (02) :329-349

[8] ELECTRON-MICROSCOPY OF RECA-DNA COMPLEXES - 2 DIFFERENT STATES, THEIR FUNCTIONAL-SIGNIFICANCE AND RELATION TO THE SOLVED CRYSTAL-STRUCTURE [J].

EGELMAN, EH ;

STASIAK, A .

MICRON, 1993, 24 (03) :309-324

[9] Exchanging partners: Recombination in E-coli [J].

Eggleston, AK ;

West, SC .

TRENDS IN GENETICS, 1996, 12 (01) :20-26

[10] Mutations in the N-terminal region of RecA that disrupt the stability of free protein oligomers but not RecA-DNA complexes [J].

Eldin, S ;

Forget, AL ;

Lindenmuth, DM ;

Logan, KM ;

Knight, KL .

JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (01) :91-101

← 1 2 3 4 →