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Molecular and Cellular Biology, September 2001, p. 6056-6065, Vol. 21, No. 17
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.17.6056-6065.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Partners of Rpb8p, a Small Subunit Shared by Yeast RNA Polymerases I, II, and III

Jean-François Briand,1 Francisco Navarro,1,dagger Peggy Rematier,1 Claire Boschiero,1 Sylvie Labarre,1 Michel Werner,1 George V. Shpakovski,1,2 and Pierre Thuriaux1,*

Service de Biochimie and Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette, France,1 and Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117871 Moscow GSP-7 V437, Russia2

Received 27 December 2000/Returned for modification 5 February 2001/Accepted 6 June 2001

Rpb8p, a subunit common to the three yeast RNA polymerases, is conserved among eukaryotes and absent from noneukaryotes. Defective mutants were found at an invariant GGLLM motif and at two other highly conserved amino acids. With one exception, they are clustered on the Rpb8p structure. They all impair a two-hybrid interaction with a fragment conserved in the largest subunits of RNA polymerases I (Rpa190p), II (Rpb1p), and III (Rpc160p). This fragment corresponds to the pore 1 module of the RNA polymerase II crystal structure and bears a highly conserved motif (P.I.KP..LW.GKQ) facing the GGLLM motif of Rpb8p. An RNA polymerase I mutant (rpa190-G728D) at the invariant glycyl of P.I.KP..LW.GKQ provokes a temperature-sensitive defect. Increasing the gene dosage of another common subunit, Rpb6p, suppresses this phenotype. It also suppresses a conditional growth defect observed when replacing Rpb8p by its human counterpart. Hence, Rpb6p and Rpb8p functionally interact in vivo. These two subunits are spatially separated by the pore 1 module and may also be possibly connected by the disorganized N half of Rpb6p, not included in the present structure data. Human Rpb6p is phosphorylated at its N-terminal Ser2, but an alanyl replacement at this position still complements an rpb6-Delta null allele. A two-hybrid interaction also occurs between Rpb8p and the product of orphan gene YGR089w. A ygr089-Delta null mutant has no detectable growth defect but aggravates the conditional growth defect of rpb8 mutants, suggesting that the interaction with Rpb8p may be physiologically relevant.

* Corresponding author. Mailing address: Service de Biochimie and Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette, France. Phone: 33.1.69 08 35 86. Fax: 33.1.69 08 47 12. E-mail: thuriaux{at}matthieu.saclay.cea.fr.

dagger Present address: Department of Experimental Biology, University of Jaén, Paraje las Lagunillas, E-23071 Jaén, Spain.

Molecular and Cellular Biology, September 2001, p. 6056-6065, Vol. 21, No. 17
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.17.6056-6065.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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