The Spliceosome: Design Principles of a Dynamic RNP Machine

被引：2003

作者：

Wahl, Markus C. ^{[1
,2
]}

Will, Cindy L.

Luehrmann, Reinhard

机构：

[1] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany

[2] Free Univ Berlin, Inst Chem & Biochem, Fachbereich Biol, AG Strukturbiochem, D-14195 Berlin, Germany

来源：

CELL | 2009年 / 136卷 / 04期

关键词：

PRE-MESSENGER-RNA; SPLICING FACTOR PRP8; 2ND CATALYTIC STEP; SM-LIKE PROTEINS; CRYSTAL-STRUCTURE; PROTEOMIC ANALYSIS; SNRNP PROTEIN; U5; SNRNP; CONFORMATIONAL REARRANGEMENT; PRP19P-ASSOCIATED COMPLEX;

D O I：

10.1016/j.cell.2009.02.009

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：

Ribonucleoproteins (RNPs) mediate key cellular functions such as gene expression and its regulation. Whereas most RNP enzymes are stable in composition and harbor preformed active sites, the spliceosome, which removes noncoding introns from precursor messenger RNAs (pre-mRNAs), follows fundamentally different strategies. In order to provide both accuracy to the recognition of reactive splice sites in the pre-mRNA and flexibility to the choice of splice sites during alternative splicing, the spliceosome exhibits exceptional compositional and structural dynamics that are exploited during substrate-dependent complex assembly, catalytic activation, and active site remodeling.

引用

页码：701 / 718

页数：18

共 138 条

[31] The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes [J].