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The structural basis for regulated assembly and function of the transcriptional activator NtrC

¹ Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA; ² Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA; ³ Integrative Biosciences Graduate Degree Program–Chemical Biology ⁴ Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA; ⁵ Department of Microbiology, University of Georgia, Athens, Georgia 30602, USA; ⁶ BioCAT at APS/Argonne National Lab, Illinois Institute of Technology, Argonne, Illinois 60439, USA

In two-component signal transduction, an input triggers phosphorylation of receiver domains that regulate the status of output modules. One such module is the AAA+ ATPase domain in bacterial enhancer-binding proteins that remodel the ⁵⁴ form of RNA polymerase. We report X-ray solution scattering and electron microscopy structures of the activated, full-length nitrogen-regulatory protein C (NtrC) showing a novel mechanism for regulation of AAA+ ATPase assembly via the juxtaposition of the receiver domains and ATPase ring. Accompanying the hydrolysis cycle that is required for transcriptional activation, we observed major order–disorder changes in the GAFTGA loops involved in ⁵⁴ binding, as well as in the DNA-binding domains.

[Keywords: NtrC; gene regulation; AAA+ ATPase assembly; transcription activation; enhancer-binding protein; two-component signal transduction]

Received February 7, 2006; revised version accepted April 4, 2006.

⁸ Corresponding authors.

E-MAIL btn1{at}psu.edu; FAX (814) 863-7024.

⁹ E-MAIL enogales{at}lbl.gov; FAX (510) 642-8806.

Supplemental material is available at http://www.genesdev.org.

Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.1418306

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