An antitermination protein engages the elongating transcription apparatus at a promoter-proximal recognition site
- PMID: 3040263
- DOI: 10.1016/0092-8674(87)90515-0
An antitermination protein engages the elongating transcription apparatus at a promoter-proximal recognition site
Abstract
As a transcriptional activator, the N protein of phage lambda acts to suppress transcription termination by recognizing a promoter-proximal site, nut, which is separated from the terminators by thousands of base pairs. We demonstrate here that N interacts with the elongating RNA polymerase in transit through the boxB domain of nut. This interaction leads to the stable association of N as an integral component of the transcription apparatus. During subsequent elongation, N translocates along with polymerase through several defined terminators positioned beyond nut. Therefore, by being an operon-specific subunit of the transcription apparatus, N presumably prevents the interaction of polymerase with termination signals.
Similar articles
-
Action of an RNA site at a distance: role of the nut genetic signal in transcription antitermination by phage-lambda N gene product.New Biol. 1990 Nov;2(11):975-91. New Biol. 1990. PMID: 2151659
-
Effects of all single base substitutions in the loop of boxB on antitermination of transcription by bacteriophage lambda's N protein.Nucleic Acids Res. 1989 Jul 25;17(14):5565-77. doi: 10.1093/nar/17.14.5565. Nucleic Acids Res. 1989. PMID: 2527353 Free PMC article.
-
Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda.Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4061-5. doi: 10.1073/pnas.92.9.4061. Proc Natl Acad Sci U S A. 1995. PMID: 7732031 Free PMC article.
-
Phage lambda and the regulation of transcription termination.Cell. 1988 Jan 15;52(1):5-6. doi: 10.1016/0092-8674(88)90523-5. Cell. 1988. PMID: 2449971 Review. No abstract available.
-
Transcription antitermination: the lambda paradigm updated.Mol Microbiol. 1995 Oct;18(2):191-200. doi: 10.1111/j.1365-2958.1995.mmi_18020191.x. Mol Microbiol. 1995. PMID: 8709839 Review.
Cited by
-
Ubiquitous transcription factors display structural plasticity and diverse functions: NusG proteins - Shifting shapes and paradigms.Bioessays. 2015 Mar;37(3):324-34. doi: 10.1002/bies.201400177. Epub 2015 Jan 15. Bioessays. 2015. PMID: 25640595 Free PMC article. Review.
-
Sequential phosphorylation of the phosphoprotein of vesicular stomatitis virus by cellular and viral protein kinases is essential for transcription activation.J Virol. 1992 Feb;66(2):1109-18. doi: 10.1128/JVI.66.2.1109-1118.1992. J Virol. 1992. PMID: 1309893 Free PMC article.
-
Evidence that the promoter can influence assembly of antitermination complexes at downstream RNA sites.J Bacteriol. 2006 Mar;188(6):2222-32. doi: 10.1128/JB.188.6.2222-2232.2006. J Bacteriol. 2006. PMID: 16513752 Free PMC article.
-
Thermus thermophilus 16S rRNA is transcribed from an isolated transcription unit.J Bacteriol. 1989 Jun;171(6):2933-41. doi: 10.1128/jb.171.6.2933-2941.1989. J Bacteriol. 1989. PMID: 2722737 Free PMC article.
-
Analysis of transcription termination signals in the nin region of bacteriophage lambda: the roc deletion.J Bacteriol. 1988 Nov;170(11):5051-8. doi: 10.1128/jb.170.11.5051-5058.1988. J Bacteriol. 1988. PMID: 2972695 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Research Materials