Ontology highlight
ABSTRACT:
SUBMITTER: Islam MN
PROVIDER: S-EPMC2863711 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Islam M Nurul MN Fox David D Guo Rong R Enomoto Takemi T Wang Weidong W
Molecular and cellular biology 20100315 10
The RecQL5 helicase is essential for maintaining genome stability and reducing cancer risk. To elucidate its mechanism of action, we purified a RecQL5-associated complex and identified its major component as RNA polymerase II (Pol II). Bioinformatics and structural modeling-guided mutagenesis revealed two conserved regions in RecQL5 as KIX and SRI domains, already known in transcriptional regulators for Pol II. The RecQL5-KIX domain binds both initiation (Pol IIa) and elongation (Pol IIo) forms ...[more]