PRP16 IS AN RNA-DEPENDENT ATPASE THAT INTERACTS TRANSIENTLY WITH THE SPLICEOSOME

被引：293
作者：
SCHWER, B
GUTHRIE, C
机构：
[1] Department of Biochemistry and Biophysics, University of California, San Francisco
来源：
NATURE | 1991年 / 349卷 / 6309期
关键词：
D O I：
10.1038/349494a0
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The assembly of the spliceosome is an ATP-dependent process. The splicing factor PRP16 contains variations of several motifs that define the eIF-4A-like ATP-dependent RNA helicase family. The protein has now been purified and shown to exhibit RNA-dependent ATPase activity. PRP16 is required specifically for the second catalytic step of the splicing reaction in vitro. This function requires ATP binding and/or hydrolysis, which appears to be concomitant with release of the protein from the spliceosome. PRP16 may be the prototype for a set of splicing factors which use ATP to drive a cycle of conformational changes.
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页码：494 / 499
页数：6
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