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Science 5 April 1985:
Vol. 228. no. 4695, pp. 91 - 93
DOI: 10.1126/science.3156406
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Articles

Science, Vol 228, Issue 4695, 91-93
Copyright © 1985 by American Association for the Advancement of Science

articles

Thermosensitivity of a DNA recognition site: activity of a truncated nutL antiterminator of coliphage lambda

SW Peltz, AL Brown, N Hasan, AJ Podhajska, and W Szybalski

Antitermination is an important transcriptional control. In bacteriophage lambda, the presence of the nut antiterminators between the promoters and terminators results in relatively unhindered transcription when the lambda N gene product and necessary host factors are supplied. This antitermination system has been rendered thermosensitivity by modification of the nut site. A fragment of lambda DNA [74 base pairs (bp) in length]that contained the 17-bp nutL core sequence, but lacked the 8-bp boxA sequence, was cloned in a pp-N-tL1-galK plasmid between the pp promoter and gene N. This fragment mediated antitermination of transcription at 30 degrees C, as measured by assaying galK gene expression in Escherichia coli. At 42 degrees C, however, antitermination at the lambda tL1 terminator was abolished. Antitermination at 42 degrees C was restored by replacing the 74-bp nutL fragment with longer sequences containing both nutL and boxA or by cloning a synthetic boxA sequence ahead of the 74-bp nutL fragment. Thus, efficient antitermination required both boxA and the 17-bp nutL core, with the latter becoming conditionally defective when the boxA sequence was deleted.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Involvement of boxA Nucleotides in the Formation of a Stable Ribonucleoprotein Complex Containing the Bacteriophage lambda  N Protein.
J. Mogridge, T.-F. Mah, and J. Greenblatt (1998)
J. Biol. Chem. 273, 4143-4148
   Abstract »    Full Text »    PDF »
A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein..
J Mogridge, T F Mah, and J Greenblatt (1995)
Genes & Dev. 9, 2831-2845
   Abstract »    PDF »
The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase..
J R Nodwell and J Greenblatt (1991)
Genes & Dev. 5, 2141-2151
   Abstract »    PDF »
Transcription-dependent competition for a host factor: the function and optimal sequence of the phage lambda boxA transcription antitermination signal..
D I Friedman, E R Olson, L L Johnson, D Alessi, and M G Craven (1990)
Genes & Dev. 4, 2210-2222
   Abstract »    PDF »


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