Format

Send to

Choose Destination
See comment in PubMed Commons below
Trends Biochem Sci. 2012 Feb;37(2):74-84. doi: 10.1016/j.tibs.2011.10.003. Epub 2011 Nov 24.

Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases.

Author information

1
Centre for Chemical Biology, Department of Chemistry, Krebs Institute, University of Sheffield, Sheffield S3 7HF, UK. j.a.grasby@sheffield.ac.uk

Abstract

Structure-specific 5'-nucleases form a superfamily of evolutionarily conserved phosphodiesterases that catalyse a precise incision of a diverse range of DNA and RNA substrates in a sequence-independent manner. Superfamily members, such as flap endonucleases, exonuclease 1, DNA repair protein XPG, endonuclease GEN1 and the 5'-3'-exoribonucleases, play key roles in many cellular processes such as DNA replication and repair, recombination, transcription, RNA turnover and RNA interference. In this review, we discuss recent results that highlight the conserved architectures and active sites of the structure-specific 5'-nucleases. Despite substrate diversity, a common gating mechanism for sequence-independent substrate recognition and incision emerges, whereby double nucleotide unpairing of substrates is required to access the active site.

PMID:
22118811
PMCID:
PMC3341984
DOI:
10.1016/j.tibs.2011.10.003
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center