Unknown

Dataset Information

0

Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.


ABSTRACT: 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.

SUBMITTER: Tauchert MJ 

PROVIDER: S-EPMC4854570 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.

Tauchert Marcel J MJ   Ficner Ralf R  

Acta crystallographica. Section F, Structural biology communications 20160422 Pt 5


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'  ...[more]

Similar Datasets

| S-EPMC4741191 | biostudies-literature
| S-EPMC8109800 | biostudies-literature
| S-EPMC4051504 | biostudies-literature
| S-EPMC9699679 | biostudies-literature
| S-EPMC7765489 | biostudies-literature
2022-11-29 | PXD033234 | Pride
2019-12-31 | GSE116834 | GEO
| S-EPMC8535861 | biostudies-literature
| S-EPMC6929035 | biostudies-literature
| S-EPMC6121465 | biostudies-literature