| People
- Faculty
- Professor:
John J. Perona |
| Field(s): |
Biological Chemistry |
 |
| Email: |
perona@chem.ucsb.edu |
| Phone: |
(805)
893-
7389 |
Fax:
(805)
893-
4120 |
| Office: |
1142C Chem |
 |
Selected
Publications |
|
Go
to Research Group website |
| Bio: |
John Perona received his doctorate in Molecular Biophysics
& Biochemistry from Yale University in 1990. His thesis
research focused on crystallization and Xray structure
determination of an aminoacyl-tRNA synthetase bound to
tRNA - the first RNA-protein complex determined at atomic
resolution. Subsequently, he worked as a postdoctoral
fellow for four years at UCSF, where he studied the mechanisms
of catalysis and substrate specificity in proteases. Dr.
Perona joined the UCSB faculty in 1994. Here his research
concentrates on the molecular mechanisms of protein synthesis
in a variety of organisms, including conventional bacteria,
humans, and methanogenic Archaea that play a central role
in mediating the global carbon cycle. He serves on the
Editorial Board for the Journal of Biological Chemistry,
and is author of 75 publications in the general fields
of macromolecular structure-function relationships and
enzyme catalysis. |
|
Current
Research
Research in our laboratory focuses on structure-function relationships
in
proteins and in tRNAs that relate to the mechanisms of protein
synthesis in
diverse organisms. We address the mechanisms of aminoacylation
by tRNA
synthetases from Escherichia coli, humans, and methanogenic
Archaea using
recombinant DNA technology, enzyme kinetics and binding studies,
Xray
crystallography, and other biophysical methods including mass
spectrometry.
Particular problems addressed here are the interdependence of
the tRNA and
amino acid specificities, the stereochemical basis for the catalytic
rate
enhancements, the role of additional domains in eukaryotic tRNA
synthetases,
and the possibilities for rational protein engineering of the
amino acid
specificities with a view towards understanding the evolutionary
development of
the genetic code.
We are also engaged in developing several new areas of research
involving
study of the unusual metabolism of methanogenic archaebacteria.
These
organisms are found in anaerobic environments and are involved,
via their
primary energy-yielding pathways, in the interconversion of
methane and carbon
dioxide gases. They play an important role in global carbon
cycling with
implications for the recently described phenomena of global
warming. In our
lab we are using bioinformatic techniques to explore the relationships
between
the primary energy metabolism of these organisms and the molecular
machinery
that translates the genetic code. We examine the roles of
enzymes involved in
the incorporation of several unusual amino acids into proteins
that are central
to methanogenesis, as well as possible interregulation of
the methanogenesis and
protein synthesis pathways. We are also interested in studying
the importance
and mechanism of tRNA modifying enzymes as related to these
central metabolic
interconversions.
|
| Selected
Research Publications |
|
Liu C, Gamper H, Shtivelband S, Hauenstein S, Perona JJ &
Hou Y-M. Quality
control of anticodon recognition by a eukaryotic aminoacyl-tRNA
synthetase. J.
Mol. Biol., in the press (2007).
|
|
Zhang C-M, Perona JJ, Ryu K, Francklyn C & Hou Y-M. Distinct
kinetic mechanisms
of the two classes of aminoacyl-tRNA synthetases. J. Mol.
Biol. 361, 300-311
(2006).
|
|
Uter NT & Perona JJ. Active site assembly in glutaminyl-tRNA
synthetase by
tRNA-mediated induced fit. Biochemistry 45, 6858-6865 (2006).
|
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Gruic-Sovulj I, Uter NT, Bullock TL & Perona JJ. tRNA-dependent
aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA
synthetase. J. Biol. Chem. 280, 23978-23986 (2005).
|
|
Hauenstein S, Zhang C-M, Hou YM & Perona JJ. Shape-selective
RNA recognition by
cysteinyl-tRNA synthetase. Nature Struct. Mol. Biol. 11, 1134-1141
(2004).
|
|
Uter NT & Perona JJ. Long-range intramolecular signalling
in a tRNA synthetase
complex revealed by pre-steady state kinetics. Proc. Natl.
Acad. Sci. USA 101,
14396-14401 (2004).
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