Protein interaction cloning in yeast of the mouse third largest RNA polymerase II subunit, mRPB31.
The cDNA encoding a protein that interacts with the mouse homologue of the yeast RNA polymerase II (polII) subunit, RPB11, and the human polII subunit, hRPB14, has been isolated by protein interaction cloning. Its deduced amino acid sequence has 96% homology to the human third largest polII subunit, hRPB33 [Pati and Weissman (1990) J. Biol. Chem. 265, 8400 8405]. Therefore, we conclude that the cloned cDNA encodes the mouse third largest polII subunit, mRPB31. Isolation of cDNA by protein interaction cloning provides evidence supporting the hypothesis, first proposed for human polII assembly [Pati (1994) Gene 145, 289-292], that the mRPB31/mRPB14 heterodimer, rather than the mRPB31 homodimer, forms in the mouse polII assembly. Indeed, in the yeast two-hybrid system, mRPB31 was shown to fail to form homodimer.
Korobko
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IV
Department of Biochemistry, Saitama Medical School, Moroyama, Iruma-gun, Japan.
Yamamoto
K
K
Nogi
Y
Y
Muramatsu
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics*; D015870:Gene Expression; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012319:RNA Polymerase II / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D015003:Yeasts / Q000235:genetics
D018076:DNA, Complementary; D012319:RNA Polymerase II