Publikationsdatum:
2017-12-08
Beschreibung:
The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, B act , C, C*, and intron lariat spliceosome complexes revealed mechanisms of 5'–splice site (ss) recognition, branching, and intron release, but lacked information on 3'-ss recognition, exon ligation, and exon release. Here we report a cryo–electron microscopy structure of the postcatalytic P complex at 3.3-angstrom resolution, revealing that the 3' ss is mainly recognized through non–Watson-Crick base pairing with the 5' ss and branch point. Furthermore, one or more unidentified proteins become stably associated with the P complex, securing the 3' exon and potentially regulating activity of the helicase Prp22. Prp22 binds nucleotides 15 to 21 in the 3' exon, enabling it to pull the intron-exon or ligated exons in a 3' to 5' direction to achieve 3'-ss proofreading or exon release, respectively.
Schlagwort(e):
Biochemistry
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Geologie und Paläontologie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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