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The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome.

Abstract：

:Metazoan spliceosomes exhibit an elaborate protein composition required for canonical and alternative splicing. Thus, the minimal set of proteins essential for activation and catalysis remains elusive. We therefore purified in vitro assembled, precatalytic spliceosomal complex B, activated B(act), and step 1 complex C from the simple eukaryote Saccharomyces cerevisiae. Mass spectrometry revealed that yeast spliceosomes contain fewer proteins than metazoans and that each functional stage is very homogeneous. Dramatic compositional changes convert B to B(act), which is composed of approximately 40 evolutionarily conserved proteins that organize the catalytic core. Additional remodeling occurs concomitant with step 1, during which nine proteins are recruited to form complex C. The moderate number of proteins recruited to complex C will allow investigations of the chemical reactions in a fully defined system. Electron microscopy reveals high-quality images of yeast spliceosomes at defined functional stages, indicating that they are well-suited for three-dimensional structure analyses.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Fabrizio P,Dannenberg J,Dube P,Kastner B,Stark H,Urlaub H,Lührmann R

doi

10.1016/j.molcel.2009.09.040

subject

Has Abstract

pub_date

2009-11-25 00:00:00

pages

593-608

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(09)00700-X

journal_volume

36

pub_type

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