Nucleic Acids Research, Vol 27, Issue 4 1047-1055, Copyright © 1999 by Oxford University Press
A Voutsina, M Riva, C Carles and D Alexandraki
ABC14.5 (Rpb8) is a eukaryotic subunit common to all three nuclear RNA
polymerases. In Saccharomyces cerevisiae, ABC14.5 (Rpb8) is essential for
cell viability, however its function remains unknown. We have cloned and
characterised the Schizosaccharomyces pombe rpb8(+) cDNA. We found that
S.pombe rpb8, unlike the similarly diverged human orthologue, cannot
substitute for S.cerevisiae ABC14. 5 in vivo. To obtain information on the
function of this RNA polymerase shared subunit we have used S.pombe rpb8 as
a naturally altered molecule in heterologous expression assays in
S.cerevisiae. Amino acid residue differences within the 67 N-terminal
residues contribute to the functional distinction of the two yeast
orthologues in S.cerevisiae. Overexpression of the S.cerevisiae largest
subunit of RNA polymerase III C160 (Rpc1) allows S.pombe rpb8 to
functionally replace ABC14.5 in S.cerevisiae, suggesting a specific genetic
interaction between the S.cerevisiae ABC14.5 (Rpb8) and C160 subunits. We
provide further molecular and biochemical evidence showing that the
heterologously expressed S.pombe rpb8 molecule selectively affects
RNApolymerase III but not RNA polymerase I complex assembly. We also report
the identification of a S.cerevisiae ABC14.5-G120D mutant which affects RNA
polymerase III.
ARTICLES
Sequence divergence of the RNA polymerase shared subunit ABC14.5 (Rpb8) selectively affects RNA polymerase III assembly in Saccharomyces cerevisiae
Foundation for Research and Technology-HELLAS, Institute of Molecular Biology and Biotechnology and Department of Biology, University of Crete, PO Box 1527, Heraklion 711 10 Crete, Greece. alexandraki@nefeli.imbb.forth.gr
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  G. M. Proshkina, E. K. Shematorova, S. A. Proshkin, C. Zaros, P. Thuriaux, and G. V. Shpakovski Ancient origin, functional conservation and fast evolution of DNA-dependent RNA polymerase III Nucleic Acids Res., July 28, 2006; 34(13): 3615 - 3624. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Kang, Y. Hu, Y. Li, X. Guo, X. Jiang, L. Lai, B. Xia, and C. Jin Structural, Biochemical, and Dynamic Characterizations of the hRPB8 Subunit of Human RNA Polymerases J. Biol. Chem., June 30, 2006; 281(26): 18216 - 18226. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Schrantz, J. d. S. Correia, B. Fowler, Q. Ge, Z. Sun, and G. M. Bokoch Mechanism of p21-activated Kinase 6-mediated Inhibition of Androgen Receptor Signaling J. Biol. Chem., January 16, 2004; 279(3): 1922 - 1931. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Q. Tan, M. H. Prysak, and N. A. Woychik Loss of the Rpb4/Rpb7 Subcomplex in a Mutant Form of the Rpb6 Subunit Shared by RNA Polymerases I, II, and III Mol. Cell. Biol., May 1, 2003; 23(9): 3329 - 3338. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J.-F. Briand, F. Navarro, P. Rematier, C. Boschiero, S. Labarre, M. Werner, G. V. Shpakovski, and P. Thuriaux Partners of Rpb8p, a Small Subunit Shared by Yeast RNA Polymerases I, II, and III Mol. Cell. Biol., September 1, 2001; 21(17): 6056 - 6065. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Huang and R. J. Maraia Comparison of the RNA polymerase III transcription machinery in Schizosaccharomyces pombe, Saccharomyces cerevisiae and human Nucleic Acids Res., July 1, 2001; 29(13): 2675 - 2690. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Kimura and A. Ishihama Involvement of multiple subunit-subunit contacts in the assembly of RNA polymerase II Nucleic Acids Res., February 15, 2000; 28(4): 952 - 959. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Rubbi, S. Labarre-Mariotte, S. Chedin, and P. Thuriaux Functional Characterization of ABC10alpha , an Essential Polypeptide Shared by All Three Forms of Eukaryotic DNA-dependent RNA Polymerases J. Biol. Chem., October 29, 1999; 274(44): 31485 - 31492. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Markov, T. Naryshkina, A. Mustaev, and K. Severinov A zinc-binding site in the largest subunit of DNA-dependent RNA polymerase is involved in enzyme assembly Genes & Dev., September 15, 1999; 13(18): 2439 - 2448. [Abstract] [Full Text]
|
|