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MAF1  -  Maf1p

Saccharomyces cerevisiae S288c

Synonyms: Repressor of RNA polymerase III transcription MAF1, YD8119.11C, YDR005C
 
 
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High impact information on MAF1

  • Furthermore, Maf1 mutants defective in full dephosphorylation display maf1Delta phenotypes and are compromised for both nuclear localization and Pol III association [1].
  • Maf1 can exist in various phosphorylation states and interacts with Pol III in a dephosphorylated state [2].
  • The MAPK gene MAF1, related to Saccharomyces cerevisiae MPK1 and Magnaporthe grisea MPS1, was isolated and functionally characterized [3].
  • These findings suggest that MAF1 is required for the early differentiation phase of appressorium formation, whereas CMK1 is involved in the maturation of appressoria [3].
  • The maf1 gene replacement mutants grew normally, but there was a significant reduction in conidiation and fungal pathogenicity [3].
 

Biological context of MAF1

  • MAF1, cloned by complementation of the ts phenotype of maf1-1, also alleviates the antisuppressor effect [4].
  • Taken together, Maf1 appears to integrate environmental conditions and signaling pathways through its phosphorylation state, with stress leading to dephosphorylation, association with Pol III at target loci, alterations in basal factor interactions, and transcriptional repression [1].
  • The maf1-delta mutation did not affect the rate of protein biosynthesis and growth at standard conditions, but resulted in temperature-sensitive growth on non-fermentable carbon sources [5].
  • Using the lacZ- luc dual gene reporter system, we detected an almost twofold diminution of UAA and UAG readthrough in maf1-delta compared with the parental strain [5].
  • Up-regulation of tRNA biosynthesis affects translational readthrough in maf1-delta mutant of Saccharomyces cerevisiae [5].
 

Physical interactions of MAF1

  • Using coimmunoprecipitation, Maf1 was found to interact with Msn5 [6].
 

Other interactions of MAF1

  • Mutation in the MAF1 gene was identified in a screen for decreased efficiency of tRNA suppressor SUP11 in the yeast Saccharomyces cerevisiae (Sc). maf1-1 mutation exerts a dual phenotypic effect: antisuppression and temperature sensitive (ts) respiratory growth [4].
  • Maf1p may play a role in the tRNA biosynthetic pathway since a fragment of the RPO31/RPC160 gene encoding the largest subunit of RNA polymerase III was cloned as a multicopy suppressor of mafl-1 [4].
  • maf1 mutation alters the subcellular localization of the Mod5 protein in yeast [7].

References

  1. Dephosphorylation and genome-wide association of Maf1 with Pol III-transcribed genes during repression. Roberts, D.N., Wilson, B., Huff, J.T., Stewart, A.J., Cairns, B.R. Mol. Cell (2006) [Pubmed]
  2. General repression of RNA polymerase III transcription is triggered by protein phosphatase type 2A-mediated dephosphorylation of Maf1. Oficjalska-Pham, D., Harismendy, O., Smagowicz, W.J., Gonzalez de Peredo, A., Boguta, M., Sentenac, A., Lefebvre, O. Mol. Cell (2006) [Pubmed]
  3. The mitogen-activated protein kinase gene MAF1 is essential for the early differentiation phase of appressorium formation in Colletotrichum lagenarium. Kojima, K., Kikuchi, T., Takano, Y., Oshiro, E., Okuno, T. Mol. Plant Microbe Interact. (2002) [Pubmed]
  4. Mutation in a new gene MAF1 affects tRNA suppressor efficiency in Saccharomyces cerevisiae. Boguta, M., Czerska, K., Zoładek, T. Gene (1997) [Pubmed]
  5. Up-regulation of tRNA biosynthesis affects translational readthrough in maf1-delta mutant of Saccharomyces cerevisiae. Kwapisz, M., Smagowicz, W.J., Oficjalska, D., Hatin, I., Rousset, J.P., Zoładek, T., Boguta, M. Curr. Genet. (2002) [Pubmed]
  6. Derepression of RNA polymerase III transcription by phosphorylation and nuclear export of its negative regulator, Maf1. Towpik, J., Graczyk, D., Gajda, A., Lefebvre, O., Boguta, M. J. Biol. Chem. (2008) [Pubmed]
  7. maf1 mutation alters the subcellular localization of the Mod5 protein in yeast. Murawski, M., Szcześniak, B., Zoładek, T., Hopper, A.K., Martin, N.C., Boguta, M. Acta Biochim. Pol. (1994) [Pubmed]
 
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