作者: Haihong Shen , Michael R. Green
DOI: 10.1016/J.MOLCEL.2004.10.021
关键词:
摘要: Serine-arginine (SR) proteins are general splicing factors and can function through binding to exonic enhancers (ESEs). SR several other mammalian contain an arginine-serine-rich (RS) domain required promote splicing. We have recently found that the ESE bound RS functions by contacting branchpoint. Here, we perform RNA-protein crosslinking experiments show branchpoint is sequentially contacted first in complex E of essential factor U2AF(65) then prespliceosome domain. Although formation prespliceosome, at least one additional protein for complete spliceosome assembly. this contacts 5' splice site specifically mature spliceosome. propose direct contact with signals a mechanism which domains