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TitleStructural insights into how Prp5 proofreads the pre-mRNA branch site.
Journal, issue, pagesNature, Vol. 596, Issue 7871, Page 296-300, Year 2021
Publish dateAug 4, 2021
AuthorsZhenwei Zhang / Norbert Rigo / Olexandr Dybkov / Jean-Baptiste Fourmann / Cindy L Will / Vinay Kumar / Henning Urlaub / Holger Stark / Reinhard Lührmann /
PubMed AbstractDuring the splicing of introns from precursor messenger RNAs (pre-mRNAs), the U2 small nuclear ribonucleoprotein (snRNP) must undergo stable integration into the spliceosomal A complex-a poorly ...During the splicing of introns from precursor messenger RNAs (pre-mRNAs), the U2 small nuclear ribonucleoprotein (snRNP) must undergo stable integration into the spliceosomal A complex-a poorly understood, multistep process that is facilitated by the DEAD-box helicase Prp5 (refs. ). During this process, the U2 small nuclear RNA (snRNA) forms an RNA duplex with the pre-mRNA branch site (the U2-BS helix), which is proofread by Prp5 at this stage through an unclear mechanism. Here, by deleting the branch-site adenosine (BS-A) or mutating the branch-site sequence of an actin pre-mRNA, we stall the assembly of spliceosomes in extracts from the yeast Saccharomyces cerevisiae directly before the A complex is formed. We then determine the three-dimensional structure of this newly identified assembly intermediate by cryo-electron microscopy. Our structure indicates that the U2-BS helix has formed in this pre-A complex, but is not yet clamped by the HEAT domain of the Hsh155 protein (Hsh155), which exhibits an open conformation. The structure further reveals a large-scale remodelling/repositioning of the U1 and U2 snRNPs during the formation of the A complex that is required to allow subsequent binding of the U4/U6.U5 tri-snRNP, but that this repositioning is blocked in the pre-A complex by the presence of Prp5. Our data suggest that binding of Hsh155 to the bulged BS-A of the U2-BS helix triggers closure of Hsh155, which in turn destabilizes Prp5 binding. Thus, Prp5 proofreads the branch site indirectly, hindering spliceosome assembly if branch-site mutations prevent the remodelling of Hsh155. Our data provide structural insights into how a spliceosomal helicase enhances the fidelity of pre-mRNA splicing.
External linksNature / PubMed:34349264 / PubMed Central
MethodsEM (single particle)
Resolution4.1 - 13.0 Å
Structure data

13028

7oqb

EMDB-13028, PDB-7oqb:
The U2 part of Saccharomyces cerevisiae spliceosomal pre-A complex (delta BS-A ACT1)
Method: EM (single particle) / Resolution: 9.0 Å

13029

7oqc

EMDB-13029, PDB-7oqc:
The U1 part of Saccharomyces cerevisiae spliceosomal pre-A complex (delta BS-A ACT1)
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-13030:
Saccharomyces cerevisiae spliceosomal pre-A complex (U257A ACT1)
Method: EM (single particle) / Resolution: 10.4 Å

EMDB-13031:
The U1 part of Saccharomyces cerevisiae spliceosomal pre-A complex (U257A)
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-13032:
The U2 part of Saccharomyces cerevisiae spliceosomal pre-A complex (U257A)
Method: EM (single particle) / Resolution: 13.0 Å

13033

7oqe

EMDB-13033, PDB-7oqe:
Saccharomyces cerevisiae spliceosomal pre-A complex (delta BS-A ACT1)
Method: EM (single particle) / Resolution: 5.9 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • Baker's yeast (brewer's yeast)
KeywordsSPLICING / S. cerevisiae / pre-A complex / Prp5 / U1 snRNP / U2 snRNP / prespliceosome

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