Mutational analysis of the functional motifs of RuvB, an AAA(+) class helicase and motor protein for Holliday junction branch migration

Citation
H. Iwasaki et al., Mutational analysis of the functional motifs of RuvB, an AAA(+) class helicase and motor protein for Holliday junction branch migration, MOL MICROB, 36(3), 2000, pp. 528-538
Citations number
45
Categorie Soggetti
Microbiology
Journal title
MOLECULAR MICROBIOLOGY
ISSN journal
0950382X → ACNP
Volume
36
Issue
3
Year of publication
2000
Pages
528 - 538
Database
ISI
SICI code
0950-382X(200005)36:3<528:MAOTFM>2.0.ZU;2-C
Abstract
Escherichia coli RuvB protein, together with RuvA, promotes branch migratio n of Holliday junctions during homologous recombination and recombination r epair. The RuvB molecular motor is an intrinsic ATP-dependent DNA helicase with a hexameric ring structure and its architecture has been suggested to be related to those of the members of the AAA(+) protein class. In this stu dy, we isolated a large number of plasmids carrying ruvB mutant genes and i dentified amino acid residues important for the RuvB functions by examining the in vivo DNA repair activities of the mutant proteins. Based on these m utational studies and amino acid conservation among various RuvBs, we ident ified 10 RuvB motifs that agreed well with the features of the AAA(+) prote in class and that distinguished the primary structure of RuvB from that of typical DNA/RNA helicases with seven conserved helicase motifs.