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题目:: Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition.
作者:: Cléry(Antoine),Sinha(Rahul),Anczuków(Olga),Corrionero(Anna),Moursy(Ahmed),Daubner(Gerrit M),Valcárcel(Juan),Krainer(Adrian R),Allain(Frédéric H-T)
状态:: 发布时间2013-07-24 , 更新时间 2016-10-19
期刊:: Proc Natl Acad Sci U S A
摘要:: Serine/arginine (SR) proteins, one of the major families of alternative-splicing regulators in Eukarya, have two types of RNA-recognition motifs (RRMs): a canonical RRM and a pseudo-RRM. Although pseudo-RRMs are crucial for activity of SR proteins, their mode of action was unknown. By solving the structure of the human SRSF1 pseudo-RRM bound to RNA, we discovered a very unusual and sequence-specific RNA-binding mode that is centered on one α-helix and does not involve the β-sheet surface, which typically mediates RNA binding by RRMs. Remarkably, this mode of binding is conserved in all pseudo-RRMs tested. Furthermore, the isolated pseudo-RRM is sufficient to regulate splicing of about half of the SRSF1 target genes tested, and the bound α-helix is a pivotal element for this function. Our results strongly suggest that SR proteins with a pseudo-RRM frequently regulate splicing by competing with, rather than recruiting, spliceosome components, using solely this unusual RRM.
语言:: eng
DOI:

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