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          Institute: MPI für medizinische Forschung     Collection: jahrbuch_2011_archival     Display Documents



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ID: 597777.0, MPI für medizinische Forschung / jahrbuch_2011_archival
The P−Loop Domain of Yeast Clp1 Mediates Interactions Between CF IA and CPF Factors in Pre−mRNA 3' End Formation
Translation of Title:The P−Loop Domain of Yeast Clp1 Mediates Interactions Between CF IA and CPF Factors in Pre−mRNA 3' End Formation
Authors:Holbein, Sandra; Scola, Simonetta; Loll, Bernhard; Dichtl, Beatriz Solange; Hübner, Wolfgang; Meinhart, Anton; Dichtl, Bernhard
Language:English
Date of Publication (YYYY-MM-DD):2011-12-22
Title of Journal:Plosone
Journal Abbrev.:PlosOne
Volume:6
Issue / Number:12
Start Page:1
End Page:10
Sequence Number of Article:e29139
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Cleavage factor IA (CF IA), cleavage and polyadenylation factor (CPF), constitute major protein complexes required for pre−mRNA 3' end formation in yeast. The Clp1 protein associates with Pcf11, Rna15 and Rna14 in CF IA but its functional role remained unclear. Clp1 carries an evolutionarily conserved P−loop motif that was previously shown to bind ATP. Interestingly, human and archaean Clp1 homologues, but not the yeast protein, carry 5' RNA kinase activity. We show that depletion of Clp1 in yeast promoted defective 3' end formation and RNA polymerase II termination; however, cells expressing Clp1 with mutant P−loops displayed only minor defects in gene expression. Similarly, purified and reconstituted mutant CF IA factors that interfered with ATP binding complemented CF IA depleted extracts in coupled in vitro transcription/3' end processing reactions. We found that Clp1 was required to assemble recombinant CF IA and that certain P−loop mutants failed to interact with the CF IA subunit Pcf11. In contrast, mutations in Clp1 enhanced binding to the 3' endonuclease Ysh1 that is a component of CPF. Our results support a structural role for the Clp1 P−loop motif. ATP binding by Clp1 likely contributes to CF IA formation and cross−factor interactions during the dynamic process of 3' end formation
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/mRNA Processing
Identifiers:LOCALID:7733
URI:http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles...
URI:http%3A%2F%2Fwww.plosone.org%2Farticle%2Finfo%253A...
URI:http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpubmed%2F22216...
DOI:10.1371%2Fjournal.pone.0029139
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