A pathway of sequential arginine-serine-rich domain-splicing signal interactions during mammalian spliceosome assembly
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Document Type
Journal ArticlePublication Date
2004-11-05Keywords
ArginineCross-Linking Reagents
Enhancer Elements, Genetic
Exons
Hela Cells
Humans
Nuclear Proteins
Plasmids
Protein Structure, Tertiary
*RNA Precursors
RNA Splicing
RNA, Messenger
Ribonucleoproteins
Serine
Signal Transduction
Spliceosomes
Transcription, Genetic
Genetics and Genomics
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Show full item recordAbstract
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.Source
Mol Cell. 2004 Nov 5;16(3):363-73. Link to article on publisher's siteDOI
10.1016/j.molcel.2004.10.021Permanent Link to this Item
http://hdl.handle.net/20.500.14038/43925PubMed ID
15525510Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.molcel.2004.10.021