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

RPA135  -  DNA-directed RNA polymerase I core subunit...

Saccharomyces cerevisiae S288c

Synonyms: A135, DNA-directed RNA polymerase I 135 kDa polypeptide, DNA-directed RNA polymerase I polypeptide 2, DNA-directed RNA polymerase I subunit RPA135, RNA polymerase I subunit 2, ...
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.

Disease relevance of RPA135

  • However, the A135-AC40 interaction is weak compared with the E. coli alpha-beta interaction, and A135 mutation that abolishes the interaction is phenotypically silent [1].

High impact information on RPA135

  • Furthermore, measurements of the exchange of A135 and A190 subunits between preexistent Pol I and newly synthesized Pol I showed that these two largest subunits of Pol I do not disassociate through many rounds of transcription in vivo [2].
  • Finally, a strain was constructed in which transcription of the SRP3 gene was controlled by the inducible GAL7 promoter [3].
  • Second, the deduced amino acid sequence contains known amino acid sequences of two tryptic peptides from the A135 subunit of RNA polymerase I purified from S. cerevisiae [3].
  • We have cloned the SRP3 gene by using its suppressor activity and determined its complete nucleotide sequence [3].
  • When this strain, which can grow on galactose but not on glucose, was shifted from galactose medium to glucose medium, a large decrease in the cellular concentration of A135 was observed by Western blot analysis [3].

Biological context of RPA135

  • In frame TGA codons were detected, which are likely to encode conserved cysteinyl residues in the putative zinc-finger region of the RPA2 gene [4].
  • No other amino acid at position 135 gave either the wild type phenotype or the normal enzyme activity of A135 [5].
  • The importance of the A135 residue was probed genetically by analysis involving both site-directed mutagenesis and randomly generated second-site intragenic suppressor mutations [5].

Associations of RPA135 with chemical compounds

  • Curiously, the essential function of the Rpa135 Zn-binding domain is not related to Zn(2+) binding per se, since replacement of only one of the four cysteine residues with alanine led to the loss of Rpa135 function [6].

Other interactions of RPA135

  • Based on these correlations, the minimal subunit composition of S. cerevisiae (and Saccharomyces carlsbergensis) RNA polymerase A was tentatively defined as A190, A135, A40, A27, A23, A19, and A14 [7].
  • Gel-filtration studies revealed an accumulation of the smaller Rpc19p-containing complex, but not of A135, in the gtr1Delta strain [8].
  • They were also found in other positions in both the RPA2 and RPB2 genes [4].
  • We also demonstrate that determinants of RNAP assembly are conserved, and that a homologue of beta Asp(1084) in A135, the beta-like subunit of yeast RNAP I, is responsible for interaction with AC40, the largest alpha-like subunit [1].

Analytical, diagnostic and therapeutic context of RPA135

  • Separation of the protein subunit components by 5% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and analysis by autoradiography and silver staining revealed that the two largest subunits (A190 and A135) were radiolabeled [9].


  1. Inter- and intrasubunit interactions during the formation of RNA polymerase assembly intermediate. Naryshkina, T., Rogulja, D., Golub, L., Severinov, K. J. Biol. Chem. (2000) [Pubmed]
  2. RNA polymerase I remains intact without subunit exchange through multiple rounds of transcription in Saccharomyces cerevisiae. Schneider, D.A., Nomura, M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  3. Suppressor analysis of temperature-sensitive mutations of the largest subunit of RNA polymerase I in Saccharomyces cerevisiae: a suppressor gene encodes the second-largest subunit of RNA polymerase I. Yano, R., Nomura, M. Mol. Cell. Biol. (1991) [Pubmed]
  4. TGA cysteine codons and intron sequences in conserved and nonconserved positions are found in macronuclear RNA polymerase genes of Euplotes octocarinatus. Kaufmann, J., Florian, V., Klein, A. Nucleic Acids Res. (1992) [Pubmed]
  5. Characterization of yeast plasma membrane H(+)-ATPase mutant pma1-A135V and its revertants. Na, S., Perlin, D.S., Seto-Young, D., Wang, G., Haber, J.E. J. Biol. Chem. (1993) [Pubmed]
  6. Role of second-largest RNA polymerase I subunit Zn-binding domain in enzyme assembly. Naryshkina, T., Bruning, A., Gadal, O., Severinov, K. Eukaryotic Cell (2003) [Pubmed]
  7. Natural variation in yeast RNA polymerase A. Formation of a mosaic RNA polymerase A in a meiotic segregant from an interspecific hybrid. Riva, M., Buhler, J.M., Sentenac, A., Fromageot, P., Hawthorne, D.C. J. Biol. Chem. (1982) [Pubmed]
  8. Association of the GTP-binding protein Gtr1p with Rpc19p, a shared subunit of RNA polymerase I and III in yeast Saccharomyces cerevisiae. Todaka, Y., Wang, Y., Tashiro, K., Nakashima, N., Nishimoto, T., Sekiguchi, T. Genetics (2005) [Pubmed]
  9. Yeast RNA polymerase I. Derivatization of the 190 and 135 subunits by 4-thiouridine monophosphate positioned uniquely at the 3' terminus of an enzyme-bound 32P-containing transcript initiated by a triribonucleotide primer on synthetic single-stranded DNA. Kelly, S., Sheng, N., Dennis, D. J. Biol. Chem. (1990) [Pubmed]
WikiGenes - Universities