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Inhibition of RNA Helicase Brr2 by the C-Terminal Tail of the Spliceosomal Protein Prp8
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Inhibition of RNA Helicase Brr2 by the C-Terminal Tail of the Spliceosomal Protein Prp8
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Inhibition of RNA Helicase Brr2 by the C-Terminal Tail of the Spliceosomal Protein Prp8
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Journal Article
Inhibition of RNA Helicase Brr2 by the C-Terminal Tail of the Spliceosomal Protein Prp8
2013
Overview
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.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Carrier Proteins - metabolism
/ Humans
/ introns
/ Mutation
/ Proteins
/ Ribonucleoprotein, U4-U6 Small Nuclear - metabolism
/ Ribonucleoprotein, U5 Small Nuclear - metabolism
/ Ribonucleoproteins, Small Nuclear - antagonists & inhibitors
/ Ribonucleoproteins, Small Nuclear - chemistry
/ Ribonucleoproteins, Small Nuclear - metabolism
/ RNA
/ Saccharomyces cerevisiae Proteins - metabolism
/ Splicing
/ Tunnels
/ Yeasts
