TY - JOUR
T1 - Bioinformatic analysis of RecQ4 helicases reveals the presence of a RQC domain and a Zn knuckle
AU - Marino, Francesca
AU - Vindigni, Alessandro
AU - Onesti, Silvia
N1 - Funding Information:
This work was supported by grants from the Associazione Italiana per la Ricerca sul Cancro (AIRC) to S.O. [ AIRC10646 ] and to A.V. [ AIRC10510 ].
PY - 2013/7
Y1 - 2013/7
N2 - 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.
AB - 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.
KW - DNA replication
KW - RQC domain
KW - RecQ helicase
KW - RecQL4
KW - Sld2
KW - Zn knuckle
UR - http://www.scopus.com/inward/record.url?scp=84876977932&partnerID=8YFLogxK
U2 - 10.1016/j.bpc.2013.02.009
DO - 10.1016/j.bpc.2013.02.009
M3 - Article
C2 - 23624328
AN - SCOPUS:84876977932
SN - 0301-4622
VL - 177-178
SP - 34
EP - 39
JO - Biophysical Chemistry
JF - Biophysical Chemistry
ER -