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Science 14 March 1997:
Vol. 275. no. 5306, pp. 1658 - 1661
DOI: 10.1126/science.275.5306.1658

Reports

Unusual Oligomerization Required for Activity of NtrC, a Bacterial Enhancer-Binding Protein

Claire Wyman, * Irene Rombel, * Anne K. North, Carlos Bustamante, dagger Sydney Kustu dagger

Nitrogen regulatory protein C (NtrC) contacts a bacterial RNA polymerase from distant enhancers by means of DNA loops and activates transcription by allowing polymerase to gain access to the template DNA strand. It was shown that NtrC from Salmonella typhimurium must build large oligomers to activate transcription. In contrast to eukaryotic enhancer-binding proteins, most of which must bind directly to DNA, some NtrC dimers were bound solely by protein-protein interactions. NtrC oligomers were visualized with scanning force microscopy. Evidence of their functional importance was provided by showing that some inactive non-DNA-binding and DNA-binding mutant forms of NtrC can cooperate to activate transcription.

I. Rombel, A. K. North, S. Kustu, Departments of Plant Biology and Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
C. Wyman, Department of Cell Biology and Genetics, Erasmus University, Rotterdam, Netherlands.
C. Bustamante, Department of Chemistry, Howard Hughes Medical Institute and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: kustu{at}mendel.berkeley.edu or carlos{at}alice.uoregon.edu


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