Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. Signal., 9 June 2009
Vol. 2, Issue 74, p. ec194
[DOI: 10.1126/scisignal.274ec194]

EDITORS' CHOICE

Protein Modification Transcriptional Repressor Dissected

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

Living organisms have quality-control mechanisms to eliminate proteins damaged by environmental stresses. In the model organism Bacillus subtilis, the transcriptional repressor CtsR controls the expression of genes that are key to the heat-shock response. CtsR is activated by the kinase McsB to allow transcription of stress-response genes; however, the mechanism of activation is unclear. Fuhrmann et al. now describe structural and biochemical studies showing that McsB inhibits DNA binding of CtsR by specifically phosphorylating arginine residues in its DNA binding domain. This study provides a basis for exploring a potential wider role of arginine phosphorylation in prokaryotic and eukaryotic transcriptional regulation.

J. Fuhrmann, A. Schmidt, S. Spiess, A. Lehner, K. Turgay, K. Mechtler, E. Charpentier, T. Clausen, McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR. Science 324, 1323–1327 (2009). [Abstract] [Full Text]

Citation: V. Vinson, Transcriptional Repressor Dissected. Sci. Signal. 2, ec194 (2009).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882