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Reference - PMID:14713954 - Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.

Reference summary

PubMed ID
PMID:14713954
Title
Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.
Authors
Xu YZ, Newnham CM, Kameoka S, Huang T, Konarska MM, Query CC
Citation
EMBO J 2004 Jan 28;23(2):376-85
Publication year
2004
Abstract
Communication between U1 and U2 snRNPs is critical during pre-spliceosome assembly; yet, direct connections have not been observed. To investigate this assembly step, we focused on Prp5, an RNA-dependent ATPase of the DExD/H family. We identified homologs of Saccharomyces cerevisiae Prp5 in humans (hPrp5) and Schizosaccharomyces pombe (SpPrp5), and investigated their interactions and function. Depletion and reconstitution of SpPrp5 from extracts demonstrate that ATP binding and hydrolysis by Prp5 are required for pre-spliceosome complex A formation. hPrp5 and SpPrp5 are each physically associated with both U1 and U2 snRNPs; Prp5 contains distinct U1- and U2-interacting domains that are required for pre-spliceosome assembly; and, we observe a Prp5-associated U1/U2 complex in S. pombe. Together, these data are consistent with Prp5 being a bridge between U1 and U2 snRNPs at the time of pre-spliceosome formation.

Annotation

GO biological process

GO:1903241 - U2-type prespliceosome assembly

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GO cellular component

GO:0071004 - U2-type prespliceosome

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GO molecular function

GO:0016887 - ATP hydrolysis activity

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GO:1990446 - U1 snRNP binding

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GO:1990447 - U2 snRNP binding

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Single locus phenotype

FYPO:0003672 - abolished ATP binding

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FYPO:0003674 - abolished ATPase activity

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FYPO:0003633 - abolished U1 snRNP binding

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FYPO:0003635 - abolished U2 snRNP binding

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FYPO:0003630 - abolished U2-type prespliceosome assembly

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FYPO:0001168 - decreased ATPase activity

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FYPO:0003634 - decreased U1 snRNP binding

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FYPO:0003636 - decreased U2 snRNP binding

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FYPO:0003631 - decreased U2-type prespliceosome assembly

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FYPO:0003673 - normal ATP binding

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