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Mutational analysis of the functional motifs of RuvB, an AAA + class helicase and motor protein for Holliday junction branch migration
Author(s) -
Iwasaki Hiroshi,
Han YongWoon,
Okamoto Takashi,
Ohnishi Takayuki,
Yoshikawa Manabu,
Yamada Kazuhiro,
Toh Hiroyuki,
Daiyasu Hiromi,
Ogura Teru,
Shinagawa Hideo
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.01842.x
Subject(s) - holliday junction , branch migration , biology , helicase , homologous recombination , genetics , dna repair , dna , rna helicase a , gene , walker motifs , rna , biochemistry , atpase , atp hydrolysis , enzyme
Escherichia coli RuvB protein, together with RuvA, promotes branch migration of Holliday junctions during homologous recombination and recombination repair. 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 study, we isolated a large number of plasmids carrying ruvB mutant genes and identified amino acid residues important for the RuvB functions by examining the in vivo DNA repair activities of the mutant proteins. Based on these mutational studies and amino acid conservation among various RuvBs, we identified 10 RuvB motifs that agreed well with the features of the AAA + protein class and that distinguished the primary structure of RuvB from that of typical DNA/RNA helicases with seven conserved helicase motifs.