QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nodwell, J R Articles by Greenblatt, J Search for Related Content PubMed PubMed Citation Articles by Nodwell, J R Articles by Greenblatt, J Social Bookmarking                   What's this?

Research Papers

The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.

Banting and Best Department of Medical Research, University of Toronto, Canada.

Abstract

The boxA and boxB components of the lambda nut site are important for transcriptional antitermination by the phage N protein. We show here that boxA and boxB RNA in N-modified transcription complexes are inaccessible to ribonucleases and have altered sensitivity to dimethylsulfate. N and NusA suffice to weakly protect boxB, independently of boxA and other factors. However, efficient protection of the entire nut site from ribonucleases requires boxA and boxB, N, NusA, NusB, S10, and NusG. Mutations in RNA polymerase, which inhibit antitermination by N in vivo, disallow protection of the nut site during transcription in vitro; therefore, the surface of RNA polymerase must coordinate the formation of complexes containing the antitermination factors and nut site RNA.

CiteULike

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. Cheeran, N. R. Kolli, and R. Sen The Site of Action of the Antiterminator Protein N from the Lambdoid Phage H-19B J. Biol. Chem., October 19, 2007; 282(42): 30997 - 31007. [Abstract] [Full Text] [PDF]

				D. L. Court, A. B. Oppenheim, and S. L. Adhya A New Look at Bacteriophage {lambda} Genetic Networks J. Bacteriol., January 15, 2007; 189(2): 298 - 304. [Full Text] [PDF]

				R. S. Washburn, D. L. Court, and M. E. Gottesman Role of an RNase III Binding Site in Transcription Termination at {lambda} nutL by HK022 Nun Protein. J. Bacteriol., October 1, 2006; 188(19): 6824 - 6831. [Abstract] [Full Text] [PDF]

				S. J. Greive, A. F. Lins, and P. H. von Hippel Assembly of an RNA-Protein Complex: BINDING OF NusB AND NusE (S10) PROTEINS TO boxA RNA NUCLEATES THE FORMATION OF THE ANTITERMINATION COMPLEX INVOLVED IN CONTROLLING rRNA TRANSCRIPTION IN ESCHERICHIA COLI J. Biol. Chem., October 28, 2005; 280(43): 36397 - 36408. [Abstract] [Full Text] [PDF]

				N. P. Johnson, W. A. Baase, and P. H. von Hippel Low Energy CD of RNA Hairpin Unveils a Loop Conformation Required for {lambda}N Antitermination Activity J. Biol. Chem., September 16, 2005; 280(37): 32177 - 32183. [Abstract] [Full Text] [PDF]

				H. C. Kim, J.-g. Zhou, H. R. Wilson, G. Mogilnitskiy, D. L. Court, and M. E. Gottesman Phage HK022 Nun protein represses translation of phage lambda N (transcription termination/translation repression) PNAS, April 29, 2003; 100(9): 5308 - 5312. [Abstract] [Full Text] [PDF]

				J. Mogridge and J. Greenblatt Specific Binding of Escherichia coli Ribosomal Protein S1 to boxA Transcriptional Antiterminator RNA J. Bacteriol., April 15, 1998; 180(8): 2248 - 2252. [Abstract] [Full Text]

				J. Mogridge, T.-F. Mah, and J. Greenblatt Involvement of boxA Nucleotides in the Formation of a Stable Ribonucleoprotein Complex Containing the Bacteriophage lambda  N Protein J. Biol. Chem., February 13, 1998; 273(7): 4143 - 4148. [Abstract] [Full Text] [PDF]

				H. R. Wilson, L. Kameyama, J.-g. Zhou, G. Guarneros, and D. L. Court Translational repression by a transcriptional elongation factor Genes & Dev., September 1, 1997; 11(17): 2204 - 2213. [Abstract] [Full Text] [PDF]

				L. Su, J. T. Radek, L. A. Labeots, K. Hallenga, P. Hermanto, H. Chen, S. Nakagawa, M. Zhao, S. Kates, and M. A. Weiss An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch Genes & Dev., September 1, 1997; 11(17): 2214 - 2226. [Abstract] [Full Text] [PDF]

				M. Krohn and R. Wagner Transcriptional Pausing of RNA Polymerase in the Presence of Guanosine Tetraphosphate Depends on the Promoter and Gene Sequence J. Biol. Chem., September 27, 1996; 271(39): 23884 - 23894. [Abstract] [Full Text] [PDF]

				J Mogridge, T F Mah, and J Greenblatt A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein. Genes & Dev., November 15, 1995; 9(22): 2831 - 2845. [Abstract] [PDF]

				J E Novak and K Kirkegaard Coupling between genome translation and replication in an RNA virus. Genes & Dev., July 15, 1994; 8(14): 1726 - 1737. [Abstract] [PDF]

				J Li, S W Mason, and J Greenblatt Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription. Genes & Dev., January 1, 1993; 7(1): 161 - 172. [Abstract] [PDF]

				C Giardina, M Perez-Riba, and J T Lis Promoter melting and TFIID complexes on Drosophila genes in vivo. Genes & Dev., November 1, 1992; 6(11): 2190 - 2200. [Abstract] [PDF]

				K. J. Harrington, R. B. Laughlin, and S. Liang Balanced branching in transcription termination PNAS, April 24, 2001; 98(9): 5019 - 5024. [Abstract] [Full Text] [PDF]