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Title3D cryo-EM structure of an active step I spliceosome and localization of its catalytic core.
Journal, issue, pagesMol Cell, Vol. 40, Issue 6, Page 927-938, Year 2010
Publish dateDec 22, 2010
AuthorsMonika M Golas / Bjoern Sander / Sergey Bessonov / Michael Grote / Elmar Wolf / Berthold Kastner / Holger Stark / Reinhard Lührmann /
PubMed AbstractThe spliceosome excises introns from pre-mRNA in a two-step splicing reaction. So far, the three-dimensional (3D) structure of a spliceosome with preserved catalytic activity has remained elusive. ...The spliceosome excises introns from pre-mRNA in a two-step splicing reaction. So far, the three-dimensional (3D) structure of a spliceosome with preserved catalytic activity has remained elusive. Here, we determined the 3D structure of the human, catalytically active step I spliceosome (C complex) by cryo-electron microscopy (cryo-EM) in vitrified ice. Via immunolabeling we mapped the position of the 5' exon. The C complex contains an unusually salt-stable ribonucleoprotein (RNP) core that harbors its catalytic center. We determined the 3D structure of this RNP core and also that of a post-step II particle, the 35S U5 snRNP, which contains most of the C complex core proteins. As C complex domains could be recognized in these structures, their position in the C complex could be determined, thereby allowing the region harboring the spliceosome's catalytic core to be localized.
External linksMol Cell / PubMed:21172658
MethodsEM (single particle)
Resolution27.8 - 29.0 Å
Structure data

EMDB-1846:
Human native spliceosomal C complex assembled on PM5 pre-mRNA.
Method: EM (single particle) / Resolution: 29.0 Å

EMDB-1847:
Human 35S U5 snRNP
Method: EM (single particle) / Resolution: 27.8 Å

EMDB-1848:
High salt resistant human spliceosomal C complex core
Method: EM (single particle)

Source
  • Homo sapiens (human)

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