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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 www.ucihs.uci.edu/pandb/
   
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

   
   
Link to this profile http://www.faculty.uci.edu/profile.cfm?faculty_id=2374
   
Last updated 05/17/2012