Advertisement
JBC

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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pati, U. K.
Right arrow Articles by Weissman, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pati, U. K.
Right arrow Articles by Weissman, S. M.
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. 265, Issue 15, 8400-8403, May, 1990

The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB 33 is highly conserved among eukaryotes

UK Pati and SM Weissman
Department of Human Genetics, Yale University School of Medicine, New Haven, Connecticut 06510.

We have cloned and sequenced a cDNA of 1766 base pairs in length encoding the 275 amino acids of hRPB 33, the third largest subunit of human RNA polymerase II. The DNA was isolated by screening of a human lambda gt11 cDNA library with oligonucleotides designed on the basis of the amino acid residue analysis of the bovine material. The hRPB 33 amino acid sequence is highly conserved between Saccharomyces cerevisiae and human. Overall, 45% of the amino acid residues are identical with the yeast homologue RPB 3, and 65% of the amino acids are identical in the two major conserved regions at residues 0-103 and 151-197. hRPB 33 is also homologous to yeast RPC 5. The amino acid sequence of hRPB 33 showed no obvious homology with bacterial RNA polymerase or with any of its sigma factors.
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
Mol. Cell. Biol.Home page
V. Khazak, J. Estojak, H. Cho, J. Majors, G. Sonoda, J. R. Testa, and E. A. Golemis
Analysis of the Interaction of the Novel RNA Polymerase II (pol II) Subunit hsRPB4 with Its Partner hsRPB7 and with pol II
Mol. Cell. Biol., April 1, 1998; 18(4): 1935 - 1945.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
J. Acker, M. de Graaff, I. Cheynel, V. Khazak, C. Kedinger, and M. Vigneron
Interactions between the Human RNA Polymerase II Subunits
J. Biol. Chem., July 4, 1997; 272(27): 16815 - 16821.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Yao, K. Yamamoto, Y. Nishi, Y. Nogi, and M. Muramatsu
Mouse RNA Polymerase I 16-kDa Subunit Able to Associate with 40-kDa Subunit Is a Homolog of Yeast AC19 Subunit of RNA Polymerases I and III
J. Biol. Chem., December 20, 1996; 271(51): 32881 - 32885.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Ulmasov, R. M. Larkin, and T. J. Guilfoyle
Association between 36- and 13.6-kDa alpha-Like Subunits of Arabidopsis thaliana RNA Polymerase II
J. Biol. Chem., March 1, 1996; 271(9): 5085 - 5094.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1990 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement