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Science 17 December 1999:
Vol. 286. no. 5448, pp. 2337 - 2339
DOI: 10.1126/science.286.5448.2337
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Reports

Binding of Transcription Termination Protein Nun to Nascent RNA and Template DNA

Randolph S. Watnick, * Max E. Gottesman dagger

The amino-terminal arginine-rich motif of coliphage HK022 Nun binds phage lambda  nascent transcript, whereas the carboxyl-terminal domain interacts with RNA polymerase (RNAP) and blocks transcription elongation. RNA binding is inhibited by zinc (Zn2+) and stimulated by Escherichia coli NusA. To study these interactions, the Nun carboxyl terminus was extended by a cysteine residue conjugated to a photochemical cross-linker. The carboxyl terminus contacted NusA and made Zn2+-dependent intramolecular contacts. When Nun was added to a paused transcription elongation complex, it cross-linked to the DNA template. Nun may arrest transcription by anchoring RNAP to DNA.

Department of Biochemistry and Molecular Biophysics and Institute of Cancer Research, Columbia University, New York, NY 10032, USA.
*   Present address: Whitehead Institute, 9 Cambridge Center, Cambridge, MA 02142, USA.

dagger    To whom correspondence should be addressed. E-mail: gottesma{at}cuccfa.ccc.columbia.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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M. A. Turnage, P. Brewer-Jensen, W.-L. Bai, and L. L. Searles (2000)
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The carboxyl terminus of phage HK022 Nun includes a novel zinc-binding motif and a tryptophan required for transcription termination.
R. S. Watnick, S. C. Herring, A. G. Palmer III, and M. E. Gottesman (2000)
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The Structure of the Coliphage HK022 Nun Protein-lambda -phage boxB RNA Complex. IMPLICATIONS FOR THE MECHANISM OF TRANSCRIPTION TERMINATION.
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