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Science 1 December 1995:
Vol. 270. no. 5241, pp. 1495 - 1497
DOI: 10.1126/science.270.5241.1495
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Reports

Solution Structure of the Activator Contact Domain of the RNA Polymerase Subunit

Young Ho Jeon,  Tomofumi Negishi,  Masahiro Shirakawa,  Toshio Yamazaki,  Nobuyuki Fujita,  Akira Ishihama (1),  Yoshimasa Kyogoku (1)

The structure of the carboxyl-terminal domain of the Escherichia coli RNA polymerase alpha subunit (alphaCTD), which is regarded as the contact site for transcription activator proteins and for the promoter UP element, was determined by nuclear magnetic resonance spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. The UP element binding site was found on the surface comprising helix 1, the amino-terminal end of helix 4, and the preceding loop. Mutation experiments indicated that the contact sites for transcription activator proteins are also on the same surface.



Y. H. Jeon, T. Yamazaki, Y. Kyogoku, Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan.
T. Negishi, N. Fujita, A. Ishihama, Department of Molecular Genetics, National Institute of Genetics, Mishima, Shizuoka 411, Japan.
M. Shirakawa, Graduate School of Bioscience, Nara Institute of Science and Technology, Takayama, Ikoma, Nara 630-01, Japan.
(1) To whom correspondence should be addressed.


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