Literature DB >> 10490594

Genetic and physical interactions involving the yeast nuclear cap-binding complex.

P Fortes1, J Kufel, M Fornerod, M Polycarpou-Schwarz, D Lafontaine, D Tollervey, I W Mattaj.   

Abstract

Yeast strains lacking the yeast nuclear cap-binding complex (yCBC) are viable, although impaired in growth. We have taken advantage of this observation to carry out a genetic screen for components that show synthetic lethality (SL) with a cbp20-Delta cbp80-Delta double mutation. One set of SL interactions was due to mutations that were complemented by components of U1 small nuclear RNP (snRNP) and the yeast splicing commitment complex. These interactions confirm the role of yCBC in commitment complex formation. Physical interaction of yCBC with the commitment complex components Mud10p and Mud2p, which may directly mediate yCBC function, was demonstrated. Unexpectedly, we identified multiple SL mutations that were complemented by Cbf5p and Nop58p. These are components of the two major classes of yeast small nucleolar RNPs, which function in the maturation of rRNA precursors. Mutants lacking yCBC were found to be defective in rRNA processing. Analysis of the yCBC deletion phenotype suggests that this is likely to be due to a defect in the splicing of a subset of ribosomal protein mRNA precursors.

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Year:  1999        PMID: 10490594      PMCID: PMC84624          DOI: 10.1128/MCB.19.10.6543

Source DB:  PubMed          Journal:  Mol Cell Biol        ISSN: 0270-7306            Impact factor:   4.272


  82 in total

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5.  Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein.

Authors:  N Kataoka; M Ohno; I Moda; Y Shimura
Journal:  Nucleic Acids Res       Date:  1995-09-25       Impact factor: 16.971

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  52 in total

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5.  RPL30 regulation of splicing reveals distinct roles for Cbp80 in U1 and U2 snRNP cotranscriptional recruitment.

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8.  Cap-binding protein 1-mediated and eukaryotic translation initiation factor 4E-mediated pioneer rounds of translation in yeast.

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