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Your search keyword '"Ebright, Richard H."' showing total 20 results
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20 results on '"Ebright, Richard H."'

16. An Open Letter to Elias Zerhouni

Author

Altman, Sidney, Bassler, Bonnie L., Beckwith, Jon, Belfort, Marlene, Berg, Howard C., Bloom, Barry, Brenchley, Jean E., Campbell, Allan, Collier, R. John, Connell, Nancy, Cozzarelli, Nicholas R., Craig, Nancy L., Darst, Seth, Ebright, Richard H., Elledge, Stephen J., Falkow, Stanley, Galan, Jorge E., Gottesman, Max, Gourse, Richard, Gross, Carol A., Grossman, Alan, Hochschild, Ann, Howe, Martha, Hurwitz, Jerard, Isberg, Ralph R., Kaplan, Samuel, Kornberg, Arthur, Kustu, Sydney G., Landick, Robert C., Landy, Arthur, Levy, Stuart B., Losick, Richard, Long, Sharon R., Maloy, Stanley R., Mekalanos, John J., Neidhardt, Frederick C., Pace, Norman R., Ptashne, Mark, Roberts, Jeffrey W., Roth, John R., Rothman-Denes, Lucia B., Salyers, Abigail, Schaechter, Moselio, Shapiro, Lucy, Silhavy, Thomas J., Simon, Melvini I., Walker, Graham, Yanofsky, Charles, and Zinder, Norton

Published
2005

19. RNA polymerase beta' subunit: a target of DNA binding-independent activation

Author

Miller, Alita, Wood, Douglas, Ebright, Richard H., and Rothman-Denes, Lucia B.

Subjects
Research, Genetic aspects, Bacteriophages -- Genetic aspects -- Research, Transcription (Genetics) -- Research -- Genetic aspects, RNA polymerases -- Research -- Genetic aspects, DNA binding proteins -- Research -- Genetic aspects, Genetic transcription -- Research -- Genetic aspects
Abstract

N4SSB, a single-stranded DNA (ssDNA) binding protein encoded by bacteriophage N4, activates transcription by the Escherichia cold [Σ.sup.70] RNA polymerase (RNAP) at N4 late promoters (1). In addition, N4SSB is [...], The bacteriophage N4 single-stranded DNA binding protein (N4SSB) activates transcription by the Escherichia coli [Σ.sup.70]-RNA polymerase at N4 late promoters. Here it is shown that the single-stranded DNA binding activity of N4SSB is not required for transcriptional activation. N4SSB interacts with the carboxyl terminus of the RNA polymerase Β' subunit in a region that is highly conserved in the largest subunits of prokaryotic and eukaryotic RNA polymerases.

Published
1997

20. Structural basis of transcription activation.

Author

Yu Feng, Yu Zhang, and Ebright, Richard H.

Subjects
*GENETIC transcription, *RNA polymerases, *ESCHERICHIA coli, *THERMUS thermophilus, *PROTEIN-protein interactions
Abstract

Class II transcription activators function by binding to a DNA site overlapping a core promoter and stimulating isomerization of an initial RNA polymerase (RNAP)- promoter closed complex into a catalytically competent RNAP-promoter open complex. Here, we report a 4.4 angstrom crystal structure of an intact bacterial class II transcription activation complex. The structure comprises Thermus thermophilus transcription activator protein TTHB099 (TAP) [homolog of Escherichia coli catabolite activator protein (CAP)], T. thermophilus RNAP σA holoenzyme, a class II TAP-dependent promoter, and a ribotetranucleotide primer. The structure reveals the interactions between RNAP holoenzyme and DNA responsible for transcription initiation and reveals the interactions between TAP and RNAP holoenzyme responsible for transcription activation. The structure indicates that TAP stimulates isomerization through simple, adhesive, stabilizing protein-protein interactions with RNAP holoenzyme. [ABSTRACT FROM AUTHOR]

Published
2016
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