The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PBP1  -  Pbp1p

Saccharomyces cerevisiae S288c

Synonyms: MRS16, PAB1-binding protein 1, YGR178C
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on PBP1

  • Tandem affinity purification linked one candidate, LSM12, to the RNA processing proteins PBP1 and PBP4 [1].
  • Loss of PBP1 resembles an mkt1 Delta deletion, causing decreased expression of HO at the posttranscriptional level [2].
  • Previously, we demonstrated that the yeast protein Pbp1p associates with poly(A)-binding protein (Pab1p) and controls the extent of mRNA polyadenylation [3].
  • Of the putative interacting genes examined, PBP1 promoted the highest level of resistance to 3-aminotriazole (>100 mM) in constructs in which HIS3 was used as a reporter [4].
  • Here, we show that, similar to Pbp1, ATX2 suppresses the petite (pet-) phenotype of Deltamrs2 yeast strains lacking mitochondrial group II introns [5].

Biological context of PBP1

  • The suppression of pab1Delta by pbp1Delta appears to be different from that mediated by other pab1 suppressors, since disruption of PBP1 does not alter translation rates, affect accumulation of ribosomal subunits, change mRNA poly(A) tail lengths, or result in a defect in mRNA decay [4].
  • Rather, Pbp1p appears to function in the nucleus to promote proper polyadenylation [4].
  • Deltapbp1Deltapbp2 and pbp1 null haploids were hypersensitive to calcineurin inhibitors, cyclosporin A and FK506, with which the mutants underwent arrest at post-anaphase and cell lysis [6].

Anatomical context of PBP1

  • We determined that a fraction of Pbp1p cosediments with polysomes in sucrose gradients and that its distribution is very similar to that of Pab1p [4].

Physical interactions of PBP1

  • Pan3p and Pbp1p both interact with themselves and with the C terminus of Pab1p [7].

Regulatory relationships of PBP1

  • These effects suggest that Pbp1p may act to repress the ability of Pab1p to negatively regulate polyadenylation [4].
  • These observations suggest that a complex of Mkt1 and Pbp1 regulates the translation of HO mRNA [2].

Other interactions of PBP1

  • Disruption of PBP1 showed that it is not essential for viability but can suppress the lethality associated with a PAB1 deletion [4].
  • Our results suggest that increased amounts of Cct6p, Ssb1p, Icy1p, Tip41p, and Pbp1p help overcome the problems resulting from a defect in protein import [8].
  • RESULTS: Two fission yeast genes pbp1+ and pbp2+ homologous to the regulatory subunit B' were isolated [6].


  1. Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Fleischer, T.C., Weaver, C.M., McAfee, K.J., Jennings, J.L., Link, A.J. Genes Dev. (2006) [Pubmed]
  2. Posttranscriptional regulation of HO expression by the Mkt1-Pbp1 complex. Tadauchi, T., Inada, T., Matsumoto, K., Irie, K. Mol. Cell. Biol. (2004) [Pubmed]
  3. Identification of factors regulating poly(A) tail synthesis and maturation. Mangus, D.A., Smith, M.M., McSweeney, J.M., Jacobson, A. Mol. Cell. Biol. (2004) [Pubmed]
  4. Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mangus, D.A., Amrani, N., Jacobson, A. Mol. Cell. Biol. (1998) [Pubmed]
  5. An integrative approach to gain insights into the cellular function of human ataxin-2. Ralser, M., Albrecht, M., Nonhoff, U., Lengauer, T., Lehrach, H., Krobitsch, S. J. Mol. Biol. (2005) [Pubmed]
  6. Fission yeast homologues of the B' subunit of protein phosphatase 2A: multiple roles in mitotic cell division and functional interaction with calcineurin. Tanabe, O., Hirata, D., Usui, H., Nishito, Y., Miyakawa, T., Igarashi, K., Takeda, M. Genes Cells (2001) [Pubmed]
  7. Positive and negative regulation of poly(A) nuclease. Mangus, D.A., Evans, M.C., Agrin, N.S., Smith, M., Gongidi, P., Jacobson, A. Mol. Cell. Biol. (2004) [Pubmed]
  8. Suppression of a defect in mitochondrial protein import identifies cytosolic proteins required for viability of yeast cells lacking mitochondrial DNA. Dunn, C.D., Jensen, R.E. Genetics (2003) [Pubmed]
WikiGenes - Universities