Larry E. Vickery


Professor Emeritus, Physiology & Biophysics
School of Medicine

PH.D., University of California, Santa Barbara

Phone: (949) 824-6580, 6541
Fax: (949) 824-8540
Email: lvickery@uci.edu

University of California, Irvine
C333, C322 MED SCI I
Mail Code: 4560
Irvine, CA 92697
Research Interests
Molecular chaperones, protein structure and folding, iron-sulfur proteins
URL
Research Abstract
The research in Dr. Vickery's laboratory is directed to providing an understanding of the roles of molecular chaperones in protein folding. Current studies are focused on the Hsc66/Hsc20 chaperone system in Escherichia coli, Saccharomyces cerevisiae, and man and their roles in the biogenesis of iron-sulfur proteins. Recent work indicates that Hsc66 and Hsc20 function together with new types of metallochaperone and metal scaffold proteins for de novo assembly of iron-sulfur clusters. Studies are underway to investigate the molecular mechanisms of iron-sulfur protein assembly, how this process is regulated, and how defects in iron-sulfur protein maturation may be linked to disturbances in iron homeostasis and diseases involving mitochondrial myopathies. The findings are also yielding molecular information into how substrate/client proteins are targeted to and recognized by molecular chaperones, and these may provide new insights into general functions of chaperone proteins in a range of human diseases.
Publications
Vickery LE, Cupp-Vickery JR. (2007) Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation. Crit. Rev. Biochem. Mol. Biol. 42, 95-111.
 
Tapley, T.L., Cupp-Vickery, J.R. & Vickery, L.E. (2006) Structural determinants of HscA peptide binding specificity. Biochemistry 45, 8058-8066.
 
Tapley, T.L., Cupp-Vickery, J.R. & Vickery, L.E. (2006) Structural determinants of HscA peptide binding specificity. Biochemistry 45, 8058-8066.
 
Tapley, T.L., Cupp-Vickery, J.R. & Vickery, L.E. (2005) Sequence-dependent peptide binding orientation by the molecular chaperone DnaK”. Biochemistry 44, 12307-12315.

Bonomi, F., Iametti, S., Ta, D.T. & Vickery, L.E. (2005) Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA”. J. Biol. Chem. 280, 29513-29518.

Aoto, P., Ta, D.T., Cupp-Vickery, J.R. & Vickery, L.E. (2005) X-ray diffraction analysis of a crystal of HscA from Escherichia coli.” Acta Crystallog. F61, 715-717.

Silberg, J.J., Tapley, T.L., Hoff, K.G. & Vickery, L.E. (2004) Regulation of the HscA ATPase reaction cycle by the cochaperone HscB and the iron-sulfur cluster assembly protein IscU”. J. Biol. Chem. 279, 53924-53931.

Cupp-Vickery, J.R., Peterson, J.C., Ta, D.T. & Vickery, L.E. (2004) Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC”, J. Mol. Biol. 342, 1265-78.

Tapley, TL. & Vickery, L.E. (2004) Preferential substrate binding orientation by the molecular chaperone HscA” , J. Biol. Chem. 279, 28435-28442.

Lauhon, C.T., Skovran, E., Urbina, H.D., Downs, D.M. & Vickery, L.E. (2004) Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo”. J. Biol. Chem. 279, 19551-19558.

Cupp-Vickery, J.R., Silberg, J.J., Ta, D.T. & Vickery, L.E. (2004) Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli”, J. Mol. Biol. 338, 127-137.

Hoff, K.G., Cupp-Vickery, J.R. & Vickery, L.E. (2003) Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system”. J.Biol. Chem. 278, 37582-37589.

Cupp-Vickery, J.R., Urbina, H.D. & Vickery, L.E. (2003) Crystal structure of IscS, a cysteine desulfurase from Escherichia coli.” J. Mol. Biol. 330, 1049-59.

Sun, G., Gargus, J.J., Ta, D.T. & Vickery, L.E. (2003) Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone.” J. Human Genetics 48, 415-419.

Hoff, K.G., Ta, D.T., Tapley, T.L., Silberg, J.J. & Vickery, L.E. (2002) Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU.” J. Biol Chem. 277, 27353-27359.

Urbina, H.D., Silberg, J.J., Hoff, K.G. & Vickery, L.E. (2001) Transfer of sulfur from IscS to IscU during iron-sulfur cluster assembly.” J. Biol. Chem. 276, 44521-44526.

Silberg, J.J., Hoff, K.G., Tapley, T.L. & Vickery, L.E. (2001) The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli.” J. Biol Chem. 276, 1696-1700.

Cupp-Vickery, J.R. & Vickery, L.E. (2000) Crystal structure of Hsc20, a J-type co-chaperone from Escherichia coli.” J. Mol. Biol. 304, 835-845.

Hoff, K.G., Silberg, J.J. & Vickery, L.E. (2000) "Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system in Escherichia coli. Proc. Natl. Acad. Sci. USA 97, 7790-7795.

Silberg, J.J. & Vickery, L.E. (2000) Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli.” J. Biol Chem. 275, 7779-7786.
Grant
NIGMS, NIH "Chaperone function and iron-sulfur protein folding"
Graduate Programs
Structural Biology and Molecular Biophysics

Last updated
05/17/2012