E. Peter Geiduschek
e-mail: epg@biomail.ucsd.edu |
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The central theme of current research
is the enzymology of gene regulation, specifically of transcriptional
regulation. Our focus is on fundamental mechanisms, approached
from a molecular genetic and biochemical perspective. It is now
widely appreciated that the transcriptional apparatus of all
cells (archaeal, bacterial and eukaryotic) has common evolutionary
roots. It follows that transcription-regulatory mechanisms should
also share certain broadly similar mechanistic features. In that
spirit, we work in parallel with bacteria and their viruses,
with eukaryotes, and with archaea.
Areas of recent, current and planned research:
1) the constitution, structure and functions of transcription
initiation complexes (transcriptional initiation is an
important, although not the exclusive,
control point of gene regulation)
2) comparison of the structures of transcription initiation complexes
formed by archaeal and eukaryotic RNA polymerases
3) regulation of transcription in archaea
4) transcriptional activation by topologically (as opposed to physically)
bound proteins.
Nechaev, S., Kamali-Moghaddam, M., André, E., Léonetti, J.-P. and Geiduschek, E.P. (2004). The T4 late transcription co-activator, gp33, binds the flap domain of Escherichia coli RNA polymerase. Proc. Natl. Acad. Sci., 101:17365-17370.
Ouhammouch, M., Langham, G.E., Hausner, W., Simpson, A.J., El-Sayed, N.M.A. and Geiduschek, E.P. (2005). Promoter architecture and response to a positive regulator of archaeal transcription. Mol. Microbiol., 56:625-637.
Kassavetis, G.A., Soragni, E., Driscoll, R. and Geiduschek, E.P. (2005). Reconfiguring the connectivity of a multiprotein complex: Fusions of yeast TBP with Brf1, and the function of TFIIIB. Proc. Natl. Acad. Sci. USA, 102:15406-15411.
Nechaev, S. and E.P. Geiduschek (2006). The role of an upstream promoter interaction in initiation of bacterial transcription. EMBO J., 25:1700-1709.
Kassavetis, G. A., Driscoll, R. and Geiduschek, E.P. (2006). Mapping the principal interaction site of the Brf1 and Bdp1 subunits of S. cerevisiae TFIIIB. J. Biol. Chem., 281:14321-14329.
Juo, Z.S., Kassavetis, G.A., Wang, J., Geiduschek, E.P. and Sigler, P.B. (2003). Crystal structure of a TFIIIB core interface ternary complex. Nature, 422:534-539.