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Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum
Author(s) -
Tauchert Marcel J.,
Ficner Ralf
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16006038
Subject(s) - spliceosome , helicase , snrnp , rna splicing , rna helicase a , thermophile , biology , small nuclear rna , rna , genetics , rna dependent rna polymerase , gene , bacteria
Prp28 (pre‐mRNA‐splicing ATP‐dependent RNA helicase 28) is a spliceosomal DEAD‐box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP‐independent manner as well as for the formation of the pre‐catalytic spliceosome, which in contrast is ATP‐dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6·U5 tri‐snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base‐pair with the 5′‐splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 Å resolution and is compared with the available structures of homologues.