HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 12, 10450-10457, March 21, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/12/10450    most recent M213310200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jourdain, S. Articles by Lefebvre, O. Search for Related Content PubMed PubMed Citation Articles by Jourdain, S. Articles by Lefebvre, O. Social Bookmarking                      What's this?

The 95 Subunit of Yeast TFIIIC Influences Upstream and Downstream Functions of TFIIIC·DNA Complexes^*

Sabine Jourdain, Joël Acker, Cécile Ducrot, André Sentenac, and Olivier Lefebvre^§

From the Service de Biochimie et de Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette Cedex, France

The yeast transcription factor IIIC (TFIIIC) is organized in two distinct multisubunit domains, A and B, that are respectively responsible for TFIIIB assembly and stable anchoring of TFIIIC on the B block of tRNA genes. Surprisingly, we found that the removal of A by mild proteolysis stabilizes the residual B·DNA complexes at high temperatures. Focusing on the well conserved 95 subunit that belongs to the A domain, we found that the 95-E447K mutation has long distance effects on the stability of TFIIIC·DNA complexes and start site selection. Mutant TFIIIC·DNA complexes presented a shift in their 5' border, generated slow-migrating TFIIIB·DNA complexes upon stripping TFIIIC by heparin or heat treatment, and allowed initiation at downstream sites. In addition, mutant TFIIIC·DNA complexes were highly unstable at high temperatures. Coimmunoprecipitation experiments indicated that 95 participates in the interconnection of A with B via its contacts with 138 and 91 polypeptides. The results suggest that 95 serves as a scaffold critical for A·DNA spatial configuration and B·DNA stability.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				H. Dumay-Odelot, C. Marck, S. Durrieu-Gaillard, O. Lefebvre, S. Jourdain, M. Prochazkova, A. Pflieger, and M. Teichmann Identification, Molecular Cloning, and Characterization of the Sixth Subunit of Human Transcription Factor TFIIIC J. Biol. Chem., June 8, 2007; 282(23): 17179 - 17189. [Abstract] [Full Text] [PDF]

				C. Ducrot, O. Lefebvre, E. Landrieux, J. Guirouilh-Barbat, A. Sentenac, and J. Acker Reconstitution of the Yeast RNA Polymerase III Transcription System with All Recombinant Factors J. Biol. Chem., April 28, 2006; 281(17): 11685 - 11692. [Abstract] [Full Text] [PDF]

				G. A. Kassavetis, E. Soragni, R. Driscoll, and E. P. Geiduschek Reconfiguring the connectivity of a multiprotein complex: Fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB PNAS, October 25, 2005; 102(43): 15406 - 15411. [Abstract] [Full Text] [PDF]

				C. Conesa, R. Ruotolo, P. Soularue, T. A. Simms, D. Donze, A. Sentenac, and G. Dieci Modulation of Yeast Genome Expression in Response to Defective RNA Polymerase III-Dependent Transcription Mol. Cell. Biol., October 1, 2005; 25(19): 8631 - 8642. [Abstract] [Full Text] [PDF]