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Science 14 March 1997: Vol. 275. no. 5306, pp. 1658 - 1661 DOI: 10.1126/science.275.5306.1658
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Reports
Unusual Oligomerization Required for Activity of NtrC, a Bacterial Enhancer-Binding Protein
Claire Wyman,
*
Irene Rombel,
*
Anne K. North,
Carlos Bustamante,
Sydney Kustu
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.
To whom correspondence should be addressed. E-mail:
kustu{at}mendel.berkeley.edu or carlos{at}alice.uoregon.edu
Read the Full Text
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