Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity

被引：110

作者：

Gu, MG

Fabrega, C

Liu, SW

Liu, HD

Kiledjian, M

Lima, CD ^{[1
]}

机构：

[1] Sloan Kettering Inst, Struct Biol Program, New York, NY 10021 USA

[2] Rutgers State Univ, Dept Cell Biol & Neurosci, Piscataway, NJ 08854 USA

来源：

MOLECULAR CELL | 2004年 / 14卷 / 01期

关键词：

D O I：

10.1016/S1097-2765(04)00180-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Complete removal of residual N-7 guanine cap from degraded messenger RNA is necessary to prevent accumulation of intermediates that might interfere with RNA processing, export, and translation. The human scavenger decapping enzyme, DcpS, catalyzes residual cap hydrolysis following mRNA degradation, releasing N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. DcpS structures bound to m(7)GpppG or m(7)GpppA reveal an asymmetric DcpS dimer that simultaneously creates an open nonproductive DcpS-cap complex and a closed productive DcpS-cap complex that alternate via 30 Angstrom domain movements. Structural and biochemical analysis suggests an autoregulatory mechanism whereby premature decapping mRNA is prevented by blocking the conformational changes that are required to form a closed productive active site capable of cap hydrolysis.

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页码：67 / 80

页数：14

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