JBC Ideal method for primary cell transfection

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wilcoxen, S. E.
Right arrow Articles by Jaehning, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wilcoxen, S. E.
Right arrow Articles by Jaehning, J. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 263, Issue 25, 12346-12351, 09, 1988

Two forms of RPO41-dependent RNA polymerase. Regulation of the RNA polymerase by glucose repression may control yeast mitochondrial gene expression

SE Wilcoxen, CR Peterson, CS Winkley, MJ Keller and JA Jaehning
Department of Biology, Indiana University, Bloomington 47405.

We have identified two chromatographically separable forms of mitochondrial RNA polymerase from Saccharomyces cerevisiae which utilize different DNA templates. One form is only active in a nonselective assay utilizing a poly[d(A-T)] template. The other form selectively initiates from a mitochondrial promoter consensus sequence. Both enzymes can be extracted from yeast mitochondria and all components are encoded by nuclear genes. The possibility that these two activities represent core and holoenzyme forms of the multicomponent mitochondrial RNA polymerase is supported by our observation that both enzymes are absent from a strain bearing a disrupted copy of the RPO41 gene (Greenleaf, A. L., Kelly, J. L., and Lehman, I. R. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 3391-3399). The two enzyme activities are differentially regulated by carbon source; the nonselective enzyme is repressed during growth on glucose relative to the selective enzyme. The 5-fold increase in RNA polymerase activity on a nonrepressing carbon source correlates with the increased level of transcript production from mitochondrial DNA. These results suggest that the mitochondrial RNA polymerase and, in consequence, mitochondrial transcription are regulated by carbon catabolite control.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Am. J. Physiol. Cell Physiol.Home page
F. Fontanesi, I. C. Soto, D. Horn, and A. Barrientos
Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process
Am J Physiol Cell Physiol, December 1, 2006; 291(6): C1129 - C1147.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
C. L. Mueller and J. A. Jaehning
Ctr9, Rtf1, and Leo1 Are Components of the Paf1/RNA Polymerase II Complex
Mol. Cell. Biol., April 1, 2002; 22(7): 1971 - 1980.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
C.-C. Chang, J. Sheen, M. Bligny, Y. Niwa, S. Lerbs-Mache, and D. B. Stern
Functional Analysis of Two Maize cDNAs Encoding T7-like RNA Polymerases
PLANT CELL, May 1, 1999; 11(5): 911 - 926.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1988 by the American Society for Biochemistry and Molecular Biology.