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Biophys Chem. 2013 Jul-Aug;177-178:34-9. doi: 10.1016/j.bpc.2013.02.009. Epub 2013 Mar 20.

Bioinformatic analysis of RecQ4 helicases reveals the presence of a RQC domain and a Zn knuckle.

Author information

1
Structural Biology Laboratory, Elettra-Sincrotrone Trieste SCpA, Area Science Park, Basovizza, Trieste, Italy. francesca.marino@elettra.trieste.it

Abstract

RecQ helicases play essential roles in the maintenance of genome stability and contain a highly conserved helicase region generally followed by a characteristic RecQ-C-terminal (RQC) domain, plus a number of variable associated domains. Notable exceptions are the RecQ4 helicases, where none of these additional regions have been described. Particularly striking was the fact that no RQC domain had been reported, considering that the RQC domain had been shown to play an essential role in the catalytic mechanism of most RecQ family members. Here we present the results of detailed bioinformatic analyses of RecQ4 proteins that identify, for the first time, the presence of a putative RQC domain, including some of the key residues involved in DNA binding and unwinding. We also describe the presence of a novel "Zn knuckle" domain, as well as an additional Sld2-homology region, providing new insights into the architecture, function and evolution of these enzymes.

PMID:
23624328
DOI:
10.1016/j.bpc.2013.02.009
[Indexed for MEDLINE]

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