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  • 标题:A close-up look at the spliceosome, at last
  • 本地全文:下载
  • 作者:John Abelson
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2017
  • 卷号:114
  • 期号:17
  • 页码:4288-4293
  • DOI:10.1073/pnas.1700390114
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Major developments in cryo-electron microscopy in the past three or four years have led to the solution of a number of spliceosome structures at high resolution, e.g., the fully assembled but not yet active spliceosome (Bact), the spliceosome just after the first step of splicing (C), and the spliceosome activated for the second step (C*). Therefore 30 years of genetics and biochemistry of the spliceosome can now be interpreted at the structural level. I have closely examined the RNase H domain of Prp8 in each of the structures. Interestingly, the RNase H domain has different and unexpected roles in each of the catalytic steps of splicing.
  • 关键词:spliceosome ; pre-mRNA splicing ; Prp8 ; RNase H ; cryo-electron microscopy
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