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TitleMechanism of spliceosome remodeling by the ATPase/helicase Prp2 and its coactivator Spp2.
Journal, issue, pagesScience, Vol. 371, Issue 6525, Year 2021
Publish dateJan 8, 2021
AuthorsRui Bai / Ruixue Wan / Chuangye Yan / Qi Jia / Jianlin Lei / Yigong Shi /
PubMed AbstractSpliceosome remodeling, executed by conserved adenosine triphosphatase (ATPase)/helicases including Prp2, enables precursor messenger RNA (pre-mRNA) splicing. However, the structural basis for the ...Spliceosome remodeling, executed by conserved adenosine triphosphatase (ATPase)/helicases including Prp2, enables precursor messenger RNA (pre-mRNA) splicing. However, the structural basis for the function of the ATPase/helicases remains poorly understood. Here, we report atomic structures of Prp2 in isolation, Prp2 complexed with its coactivator Spp2, and Prp2-loaded activated spliceosome and the results of structure-guided biochemical analysis. Prp2 weakly associates with the spliceosome and cannot function without Spp2, which stably associates with Prp2 and anchors on the spliceosome, thus tethering Prp2 to the activated spliceosome and allowing Prp2 to function. Pre-mRNA is loaded into a featured channel between the N and C halves of Prp2, where Leu from the N half and Arg from the C half prevent backward sliding of pre-mRNA toward its 5'-end. Adenosine 5'-triphosphate binding and hydrolysis trigger interdomain movement in Prp2, which drives unidirectional stepwise translocation of pre-mRNA toward its 3'-end. These conserved mechanisms explain the coupling of spliceosome remodeling to pre-mRNA splicing.
External linksScience / PubMed:33243853
MethodsEM (single particle)
Resolution2.5 - 3.2 Å
Structure data

30637

7dco

EMDB-30637, PDB-7dco:
Cryo-EM structure of the activated spliceosome (Bact complex) at an atomic resolution of 2.5 angstrom
Method: EM (single particle) / Resolution: 2.5 Å

30638

7dcp

EMDB-30638, PDB-7dcp:
cryo-EM structure of the DEAH-box helicase Prp2 and coactivator Spp2
Method: EM (single particle) / Resolution: 3.15 Å

30639

7dcq

EMDB-30639, PDB-7dcq:
cryo-EM structure of the DEAH-box helicase Prp2
Method: EM (single particle) / Resolution: 2.9 Å

30640

7dcr

EMDB-30640, PDB-7dcr:
cryo-EM structure of the DEAH-box helicase Prp2 in complex with its coactivator Spp2
Method: EM (single particle) / Resolution: 3.15 Å

30643

7dd3

EMDB-30643, PDB-7dd3:
Cryo-EM structure of the pre-mRNA-loaded DEAH-box ATPase/helicase Prp2 in complex with Spp2
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE / Phytic acid

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsSPLICING / RNA splicing / spliceosome / Bact complex / Prp2 / Spp2 / ATPase/helicase / activation / DEAH-box ATPase/helicase

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