Award Abstract #0710816
International Research Fellowship Program: Physical Basis for Transcriptional Regulation in Bacilli

NSF Org:	OISE Office of International Science and Engineering
Initial Amendment Date:	June 13, 2007
Latest Amendment Date:	June 13, 2007
Award Number:	0710816
Award Instrument:	Fellowship
Program Manager:	Susan Parris OISE Office of International Science and Engineering O/D OFFICE OF THE DIRECTOR
Start Date:	August 1, 2007
Expires:	July 31, 2009 (Estimated)
Awarded Amount to Date:	$91340
Investigator(s):	Matthew Ferguson ferguson@physics.umd.edu (Principal Investigator)
Sponsor:	Ferguson Matthew L Chevy Chase, MD 20815 / -
NSF Program(s):	EAPSI
Field Application(s):	0000099 Other Applications NEC
Program Reference Code(s):	OTHR, 5980, 5979, 5956, 5918, 0000
Program Element Code(s):	7316

ABSTRACT

0710816

Ferguson

The International Research Fellowship Program enables U.S. scientists and engineers to conduct nine to twenty-four months of research abroad. The program's awards provide opportunities for joint research, and the use of unique or complementary facilities, expertise and experimental conditions abroad.

This award will support a twenty-four-month research fellowship by Dr. Matthew L. Ferguson to work with Dr. Cathrine Royer at the Centre de Biochimie Structurale, CNRS, in Montpellier, France.

The primary goal of this project is to better understand the interplay between structure, dynamics and energetics in transcriptional regulation in Bacilli. Cell differentiation and growth can be controlled at the level of transcription of DNA to mRNA. This process is mediated by a number of protein-protein and protein-DNA complexes, in addition to that between the RNA polymerase and the gene and transcript. Proteins that serve to modulate gene transcription are called transcription factors. Modulation of the expression of genes by these factors occurs through their ability to enhance (activation) or disfavor (repression) recruitment of the proteins involved in the transcription. This process involves specific, high affinity interactions both protein-protein and protein-DNA. Determining the structural and energetic basis for the affinity and specificity of these interactions is important for the understanding of transcriptional control.

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