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A pathway of sequential arginine-serine-rich domain-splicing signal interactions during mammalian spliceosome assembly.

Abstract：

:Serine-arginine (SR) proteins are general splicing factors and can function through binding to exonic splicing enhancers (ESEs). SR proteins and several other mammalian splicing factors contain an arginine-serine-rich (RS) domain required to promote splicing. We have recently found that the ESE bound RS domain functions by contacting the branchpoint. Here, we perform RNA-protein crosslinking experiments to show that the branchpoint is sequentially contacted first in complex E by the RS domain of the essential splicing factor U2AF(65) and then in the prespliceosome by the ESE bound RS domain. Although the ESE bound RS domain can promote formation of the prespliceosome, at least one additional SR protein is required for complete spliceosome assembly. We show that the RS domain of this additional SR protein contacts the 5' splice site specifically in the mature spliceosome. We propose that direct contact with splicing signals is a general mechanism by which RS domains promote splicing.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Shen H,Green MR

doi

10.1016/j.molcel.2004.10.021

subject

Has Abstract

pub_date

2004-11-05 00:00:00

pages

363-73

issue

3

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(04)00637-9

journal_volume

16

pub_type

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