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The archaeal Hjm helicase has recQ‐like functions, and may be involved in repair of stalled replication fork
Author(s) -
Fujikane Ryosuke,
Shinagawa Hideo,
Ishino Yoshizumi
Publication year - 2006
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2006.00925.x
Subject(s) - biology , fork (system call) , replication (statistics) , helicase , recq helicase , genetics , virology , gene , computer science , rna , operating system
The archaeal Hjm is a structure‐specific DNA helicase, which was originally identified in the hyperthermophilic archaeon, Pyrococcus furiosus , by in vitro screening for Holliday junction migration activity. Further biochemical analyses of the Hjm protein from P. furiosus showed that this protein preferably binds to fork‐related Y‐structured DNAs and unwinds their double‐stranded regions in vitro , just like the E. coli RecQ protein. Furthermore, genetic analyses showed that Hjm produced in E. coli cells partially complemented the defect of functions of RecQ in a recQ mutant E. coli strain. These results suggest that Hjm may be a functional counterpart of RecQ in Archaea, in which it is necessary for the maintenance of genome integrity, although the amino acid sequences are not conserved. The functional interaction of Hjm with PCNA for its helicase activity further suggests that the Hjm works at stalled replication forks, as a member of the reconstituted replisomes to restart replication.