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| DOMAIN ORGANIZATION OF RNA-POLYMERASE ALPHA-SUBUNIT - C-TERMINAL-85 AMINO-ACIDS CONSTITUTE A DOMAIN CAPABLE OF DIMERIZATION AND DNA-BINDING |
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| Author(s): BLATTER EE, ROSS W, TANG H, GOURSE RL, EBRIGHT RH |
| Source: CELL Volume: 78 Issue: 5 Pages: 889-896 Published: SEP 9 1994 |
| Times Cited: 168 References: 44 |
| Abstract: Using limited proteolysis, we show that the Escherichia coli RNA polymerase alpha subunit consists of an N-terminal domain comprised of amino acids 8-241, a C-terminal domain comprised of amino acids 249-329, and an unstructured and/or flexible interdomain linker. We have carried out a detailed structural and functional analysis of an 85 amino acid proteolytic fragment corresponding to the C-terminal domain (alpha CTD-2). Our results establish that alpha CTD-2 has a defined secondary structure (similar to 40% alpha helix, similar to 0% beta sheet). Our results further establish that alpha CTD-2 is a dimer and that alpha CTD-2 exhibits sequence-specific DNA binding activity. Our results suggest a model for the mechanism of involvement of alpha in transcription activation by promoter upstream elements and upstream-binding activator proteins. |
| Document Type: Article |
| Language: English |
| Reprint Address: BLATTER, EE (reprint author), RUTGERS STATE UNIV, DEPT CHEM, NEW BRUNSWICK, NJ 08855 USA |
Addresses:
1. RUTGERS STATE UNIV, WAKSMAN INST, NEW BRUNSWICK, NJ 08855 USA
2. UNIV WISCONSIN, DEPT BACTERIOL, MADISON, WI 53706 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: PG296 |
| ISSN: 0092-8674 |
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