Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (353K) Freely available
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Singh, S. R.
Right arrow Articles by Sadhale, P. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Singh, S. R.
Right arrow Articles by Sadhale, P. P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 2 January 2004

Nucleic Acids Research, 2004, Vol. 32, No. 1 201-210
© 2004 Oxford University Press

Domainal organization of the lower eukaryotic homologs of the yeast RNA polymerase II core subunit Rpb7 reflects functional conservation

Sunanda R. Singh, Nambudiry Rekha1, Beena Pillai, Vijender Singh, Aruna Naorem, Vinaya Sampath, N. Srinivasan1 and Parag P. Sadhale*

Department of Microbiology and Cell Biology and 1 Molecular Biophysics Unit, Indian Institute of Science, Bangalore-12, India

*To whom correspondence should be addressed. Tel: +91 80 3942292; Fax: +91 80 3602697; Email: pps{at}mcbl.iisc.ernet.in
Present address:
B. Pillai, Institute for Genomics and Integrative Biology, New Delhi-7, India

The subcomplex of Rpb4 and Rpb7 subunits of RNA pol II in Saccharomyces cerevisiae is known to be an important determinant of transcription under a variety of physiological stresses. In S.cerevisiae, RPB7 is essential for cell viability while rpb4 null strains are temperature sensitive at low and high temperatures. The rpb4 null strain also shows defect in sporulation and a predisposed state of pseudohyphal growth. We show here that, apart from S.cerevisiae Rpb7, the Rpb7 homologs from other lower eukaryotes like Schizosaccharomyces pombe, Candida albicans and Dictyostelium discoideum can complement for the absence of S.cerevisiae RPB7. This is the first report where we have shown that both the C.albicans and D.discoideum homologs are functional orthologs of the yeast RPB7. We also show that high expression levels of S.cerevisiae RPB7 and its homologs rescue the sporulation defect of rpb4 homozygous null diploids, but only some of them cause significant enhancement of the pseudohyphal phenotype. Structural modeling of Rpb7 and its homologs show a high degree of conservation in the overall structure. This study indicates a structural and functional conservation of different Rpb7 across species and also a conserved role of Rpb7 in the subcomplex with respect to nutritional stress.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. K. Ghosh, G. Ramakrishnan, and R. Rajasekharan
YLR099C (ICT1) Encodes a Soluble Acyl-CoA-dependent Lysophosphatidic Acid Acyltransferase Responsible for Enhanced Phospholipid Synthesis on Organic Solvent Stress in Saccharomyces cerevisiae
J. Biol. Chem., April 11, 2008; 283(15): 9768 - 9775.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Sampath, B. Balakrishnan, J. Verma-Gaur, S. Onesti, and P. P. Sadhale
Unstructured N Terminus of the RNA Polymerase II Subunit Rpb4 Contributes to the Interaction of Rpb4{middle dot}Rpb7 Subcomplex with the Core RNA Polymerase II of Saccharomyces cerevisiae
J. Biol. Chem., February 15, 2008; 283(7): 3923 - 3931.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.