期刊
SCIENCE
卷 341, 期 6141, 页码 80-84出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1237515
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资金
- Helmholtz Zentrum Berlin fur Materialien und Energie
- Freie Universitat Berlin
- Humboldt-Universitat zu Berlin
- Max-Delbruck-Centrum
- Leibniz-Institut fur Molekulare Pharmakologie
- Deutsche Forschungsgemeinschaft [SFB 860, SFB 740/2]
The Ski2-like RNA helicase Brr2 is a core component of the spliceosome that must be tightly regulated to ensure correct timing of spliceosome activation. Little is known about mechanisms of regulation of Ski2-like helicases by protein cofactors. Here we show by crystal structure and biochemical analyses that the Prp8 protein, a major regulator of the spliceosome, can insert its C-terminal tail into Brr2's RNA-binding tunnel, thereby intermittently blocking Brr2's RNA-binding, adenosine triphosphatase, and U4/U6 unwinding activities. Inefficient Brr2 repression is the only recognizable phenotype associated with certain retinitis pigmentosa-linked Prp8 mutations that map to its C-terminal tail. Our data show how a Ski2-like RNA helicase can be reversibly inhibited by a protein cofactor that directly competes with RNA substrate binding.
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