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High‐resolution structure of the E.coli RecQ helicase catalytic core
Author(s) -
Bernstein Douglas A.,
Zittel Morgan C.,
Keck James L.
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg500
Subject(s) - biology , recq helicase , helicase , bloom syndrome , genetics , dna , genome instability , gene , dna damage , rna
RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 Å resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 Å resolution structure of the core bound to the ATP analog ATPγS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn 2+ ‐binding and winged‐helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ‐associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.