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RPC31  -  Rpc31p

Saccharomyces cerevisiae S288c

Synonyms: ACP2, C31, DNA-directed RNA polymerase III 31 kDa polypeptide, DNA-directed RNA polymerase III subunit RPC7, N1769, ...
 
 
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Disease relevance of RPC31

  • The two monoclonals were directed against the gp160 env protein of HIV, DZ directed against the gp41 and C31 directed against the gp120 [1].
 

High impact information on RPC31

  • The C31 subunit belongs to a complex of three subunits (C31, C34 and C82) specific to RNA polymerase (pol) III that have no counterparts in other RNA polymerases [2].
  • Of eight RNA polymerase C genes tested, only the RPC31 gene on a multicopy plasmid was capable of suppressing the rpc82(Ts) defect, suggesting an interaction between the polymerase C 82-kDa and 31-kDa subunits [3].
  • Thus, ACP2 and RPC31 are allelic and encode a subunit of RNA polymerase C. The c31 protein has a highly acidic C-terminal tail also found in several other chromatin-interacting proteins, including animal HMG1 [4].
  • Random mutagenesis failed to yield temperature-sensitive mutants, but a slowly growing mutant was constructed by partial suppression of a UAA nonsense allele of RPC31 [4].
  • Its coding sequence perfectly matches the amino acid sequence of two oligopeptides prepared from purified C31 [4].
 

Biological context of RPC31

  • Except for subunit Rpc31, this also extended to the much more distantly related genomes of Alveolates and Excavates, indicating that the complex subunit organization of RNA polymerase III emerged at a very early stage of eukaryotic evolution [5].
  • The growth phenotypes of a gene deletion, of insertions, and of nonsense mutations indicate that the C31 protein is strictly required for cell growth and that most of the acidic domain is essential for its function [4].
  • Standard procedures were used to construct a diploid yeast strain in which one copy of the ACP2 gene was mutated by replacement with the URA3 gene [6].
  • None of the viable spores contained the mutant ACP2 gene, thus proving that the protein encoded by ACP2 is required for cell viability [6].
 

Other interactions of RPC31

  • DNA sequencing and Northern (RNA) blot analysis revealed that one gene, called ACP2 (acidic protein 2), synthesizes a poly(A)+ RNA in S. cerevisiae which encodes a 27,000-molecular-weight protein whose amino acid sequence is homologous to those of calf HMG1 and HMG2 and trout HMGT proteins [6].

References

  1. Characterization and large production of human monoclonal antibodies against the HIV-1 envelope. Boyer, V., Broly, H., Souche, S., Madaule, P., Rossier, J., Zagury, D., Desgranges, C. Clin. Exp. Immunol. (1991) [Pubmed]
  2. A mutation in the C31 subunit of Saccharomyces cerevisiae RNA polymerase III affects transcription initiation. Thuillier, V., Stettler, S., Sentenac, A., Thuriaux, P., Werner, M. EMBO J. (1995) [Pubmed]
  3. RPC82 encodes the highly conserved, third-largest subunit of RNA polymerase C (III) from Saccharomyces cerevisiae. Chiannilkulchai, N., Stalder, R., Riva, M., Carles, C., Werner, M., Sentenac, A. Mol. Cell. Biol. (1992) [Pubmed]
  4. The RPC31 gene of Saccharomyces cerevisiae encodes a subunit of RNA polymerase C (III) with an acidic tail. Mosrin, C., Riva, M., Beltrame, M., Cassar, E., Sentenac, A., Thuriaux, P. Mol. Cell. Biol. (1990) [Pubmed]
  5. Ancient origin, functional conservation and fast evolution of DNA-dependent RNA polymerase III. Proshkina, G.M., Shematorova, E.K., Proshkin, S.A., Zaros, C., Thuriaux, P., Shpakovski, G.V. Nucleic Acids Res. (2006) [Pubmed]
  6. The Saccharomyces cerevisiae ACP2 gene encodes an essential HMG1-like protein. Haggren, W., Kolodrubetz, D. Mol. Cell. Biol. (1988) [Pubmed]
 
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