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RPA14  -  DNA-directed RNA polymerase I subunit RPA14

Saccharomyces cerevisiae S288c

Synonyms: A14, DNA-directed RNA polymerase I 14 kDa polypeptide, YD8358.11, YDR156W
 
 
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High impact information on RPA14

  • A protruding protein density named stalk was found to contain the RNA pol I-specific subunits A43 and A14 [1].
  • In this paper, using biochemical and genetic approaches, we demonstrate that the A43 polypeptide forms a stable heterodimer with the A14 pol I subunit and interacts with the common ABC23 subunit, the yeast counterpart of the omega subunit of bacterial RNA polymerase [2].
  • A34.5 (but not A14) becomes quasi-essential in strains lacking DNA topoisomerase I, suggesting a specific role of this subunit in helping Pol I to overcome the topological constraints imposed on ribosomal DNA by transcription [3].
  • Although no homolog of A14 has previously been found in the S. pombe genome, functional characterization of Ker1p and alignment of Ker1p and A14 showed that Ker1p is an ortholog of A14 [4].
  • Based on the amino acid sequence of one of the resulting peptides, a degenerate oligonucleotide was synthesized and used to isolate the RPA14 gene from a yeast subgenomic DNA library [5].
 

Biological context of RPA14

  • The same motif is also seen in the structure of the F subunit, suggesting a structural link between A14 and the RPB4/C17/subunit F family, even in the absence of direct sequence homology [6].
  • As examples of bases that can participate in tertiary interactions, the crystal structures show A14 and G15 in special base-pairing arrangements [7].
  • Cytoplasmic and mitochondrial enzymes catalyze the methylation (into m5C) of C48 present in the extra-loop, while chloroplast enzyme preparations catalyze the modification (into m1A) of A14 present in the dihydrouridine loop of tRNAPhe [8].
 

Associations of RPA14 with chemical compounds

  • 5. Without the two Saccharomyces species, S. cerevisiae and S. douglasii, 7 of 13 polypeptides of enzyme A(A49, A43, A40, A34.5, A19, A14.5, and A14) differ slightly in molecular weight and can be resolved by electrophoresis on polyacrylamide gel [9].
  • The exchange rates in zero spermidine and Mg++ indicate early melting of the U8 A14 interaction, in accord with thermodynamic melting studies [10].
 

Physical interactions of RPA14

  • To shed light on the function of the heterodimer, we performed gel mobility shift assays and showed that the A14/A43 heterodimer binds single-stranded RNA in a similar way to the archaeal E/F complex [6].
 

Other interactions of RPA14

  • After two purification steps, the enzyme did not contain the subunits A14, ABC23, and A43 [5].
  • 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 [9].
 

Analytical, diagnostic and therapeutic context of RPA14

  • The A14 polypeptide was separated from the other RNA polymerase I subunits by reverse-phase high pressure liquid chromatography and digested with proteinase K [5].
  • Dynamic light-scattering (DLS) analysis was used to improve the purification, stabilization and crystallization of RPA14/32 [11].

References

  1. Localization of the yeast RNA polymerase I-specific subunits. Bischler, N., Brino, L., Carles, C., Riva, M., Tschochner, H., Mallouh, V., Schultz, P. EMBO J. (2002) [Pubmed]
  2. The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship to Rpb4-Rpb7 pol II subunits. Peyroche, G., Levillain, E., Siaut, M., Callebaut, I., Schultz, P., Sentenac, A., Riva, M., Carles, C. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. A34.5, a nonessential component of yeast RNA polymerase I, cooperates with subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis machine. Gadal, O., Mariotte-Labarre, S., Chedin, S., Quemeneur, E., Carles, C., Sentenac, A., Thuriaux, P. Mol. Cell. Biol. (1997) [Pubmed]
  4. The fission yeast protein Ker1p is an ortholog of RNA polymerase I subunit A14 in Saccharomyces cerevisiae and is required for stable association of Rrn3p and RPA21 in RNA polymerase I. Imazawa, Y., Hisatake, K., Mitsuzawa, H., Matsumoto, M., Tsukui, T., Nakagawa, K., Nakadai, T., Shimada, M., Ishihama, A., Nogi, Y. J. Biol. Chem. (2005) [Pubmed]
  5. The association of three subunits with yeast RNA polymerase is stabilized by A14. Smid, A., Riva, M., Bouet, F., Sentenac, A., Carles, C. J. Biol. Chem. (1995) [Pubmed]
  6. Structural and functional homology between the RNAP(I) subunits A14/A43 and the archaeal RNAP subunits E/F. Meka, H., Daoust, G., Arnvig, K.B., Werner, F., Brick, P., Onesti, S. Nucleic Acids Res. (2003) [Pubmed]
  7. Rate of tritium labeling of specific purines in relation to nucleic acid and particularly transfer RNA conformation. Gamble, R.C., Schoemaker, J.P. Biochemistry (1976) [Pubmed]
  8. Methylation of yeast tRNAPhe by enzymes from cytoplasm, chloroplasts and mitochondria of Phaseolus vulgaris. Montasser Kouhsari, S., Keith, G., Weil, J.H. Biochim. Biophys. Acta (1978) [Pubmed]
  9. 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]
  10. Proton exchange rates in transfer RNA as a function of spermidine and magnesium. Tropp, J.S., Redfield, A.G. Nucleic Acids Res. (1983) [Pubmed]
  11. Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association. Habel, J.E., Ohren, J.F., Borgstahl, G.E. Acta Crystallogr. D Biol. Crystallogr. (2001) [Pubmed]
 
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