Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases.
Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases.
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DOI:
10.1016/j.tibs.2011.10.003
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发表时间:
2012-02
影响因子:
13.8
通讯作者:
Tainer, John A.
中科院分区:
文献类型:
--
作者:
Grasby, Jane A.;Finger, L. David;Tsutakawa, Susan E.;Atack, John M.;Tainer, John A.
Structure-specific 5′-nucleases, exemplified by the flap endonucleases (FENs), are a superfamily of evolutionarily conserved phosphodiesterases that catalyze the precise incision of a diverse range of DNA and RNA substrates. Superfamily members, that include FENs, EXO1, XPG, GEN1 and the XRNs, play key roles in many cellular processes such as DNA replication, DNA repair, recombination, transcription, RNA turnover and RNA interference. In this review we discuss recent results that show conserved architectures and active sites for members of the 5′-nuclease superfamily. Despite substrate diversity, this analysis suggests a common unified mechanism for sequence-independent substrate recognition and incision. The emerging superfamily hallmark is a surprising gating mechanism whereby double nucleotide unpairing of substrates is required to access the active site.
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