TY - JOUR
T1 - Unpairing and gating
T2 - Sequence-independent substrate recognition by FEN superfamily nucleases
AU - Grasby, Jane A.
AU - Finger, L. David
AU - Tsutakawa, Susan E.
AU - Atack, John M.
AU - Tainer, John A.
N1 - Funding Information:
We thank colleagues working on 5′-nucleases for stimulating insights, inspiration and discussions. Our work is supported by BBSRC grant BBF0147321 (JAG), FP7-Marie Curie International Incoming Fellowship Project No. 254386 (LDF) and National Cancer Institute grants RO1CA081967 and P01CA092584 (JAT).
PY - 2012/2
Y1 - 2012/2
N2 - 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.
AB - 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.
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U2 - 10.1016/j.tibs.2011.10.003
DO - 10.1016/j.tibs.2011.10.003
M3 - Review article
C2 - 22118811
AN - SCOPUS:84856699863
SN - 0968-0004
VL - 37
SP - 74
EP - 84
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 2
ER -