SAUER LAB

BIOLOGY DEPARTMENT
Alumni (2014-2011)
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JASON SELLO

JasonSello

 

Jason Sello
Martin Luther King, Jr. Visiting Associate Professor (September 2013 -
July 2014)
Email (jsello [at] mit.edu)

Faculty
Brown University
Department of Chemistry

 

Carney, D.W., Compton, C.L., Schmitz, K.R., Stevens, J.P., Sauer, R.T. & Jason K. Sello (2014) A simple fragment of the acyldepsipeptide antibacterial agents is necessary and sufficient for ClpP activation and antibacterial activity. Chembiochem. (in press).

Carney, D., Schmitz, K.R., Truong, J., Sauer, R.T., and Sello, J.K. (2014) Restriction of the conformational dynamics of the cyclic acyldepsipeptide macrocycle improves antibacterial activity by enhancing both ClpP peptidase binding and activation. J. Amer. Chem. Soc. 136, 1922-1929.

 


SEOKHEE KIM

SEOKHEEKIM

Seokhee Kim

Postdoc Associate (2008 - June 2012) and Postdoctoral Fellow (July 2012-January 2014) The Medical Foundation

Faculty
Seoul National University
Department of Chemistry



SKimImage

 

 

Kim S, Sauer RT. (2014) Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress. Genes Dev. 2014 Apr 15;28(8):902-11. doi: 10.1101/gad.238394.114. PMID: 24736846

Kim, S. & Sauer, R.T. (2012) Cage assembly of DegP protease is not required for substrate-dependent regulation of Proteolytic activity or high-temperature cell survival. Proc. Natl. Acad. Sci. USA 109(19):7263-7268. Epub 2012 April 23. PMID 22529381 [Indexed for MEDLINE] PMCID: PMC3358883.

Kim, S., Grant, R.A. & Sauer, R. T. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.Cell. 2011 Apr 1;145(1):67-78. PubMed PMID: 21458668; PubMed Central PMCID: PMC3075617.

 

 

 

MATTHEW WOHLEVER

MATTHEW WOHLEVER

Matthew L. Wohlever
National Science Foundation
Graduate Research Fellow (2009-2012)
and
Graduate Student (June 2009 - May 2013)
Visiting Scientist through July 2013

Email (wohlever[at] uchicago.edu)

Postdoctoral Scholar
University of Chicago
Gordon Center for Integrative Science
Keenan Lab


RESEARCH IMAGE

 

 

Gora, K.G., Cantin, A., Wohlever, M., Joshi, K.K., Perchuk, B.S., Chien, P., Laub, M.T. (2013) Regulated proteolysis of a transcription factor complex is critical to cell cycle progression in Caulobacter crescentus. Mol Microbiol Mar; 87(6) 1277-89, PMID 23368090.

Hesse, W.R., Steiner, M., Wohlever, M.L., Kamm, R.D., Hwang, W., and Lang, M.J. (2013) Modular aspects of kinesin force generation machinery. Biophys J. PMID 23663840.

Vieux, E.F., Wohlever, M.L., Chen, J.Z., Sauer, R.T. & Baker, T.A. (2013) Distinct quaternary structures of the AAA+ Lon protease control substrate degradation. Proc. Natl. Acad. Sci. USA.

Wohlever ML, Nager AR, Baker TA . & Sauer, RT (2013) Engineering fluorescent protein substrates for the AAA+ Lon Protease . Protein Eng Des Sei - Epub 2013. January 28. PMID 23359718.

 

 

 

 

ANDREW R. "DREW" NAGER

 

ANDREWNAGER

 

Andrew R. Nager
Graduate Student (2009-2012)
Visiting Scientist through February 2013

Email (andrewrn [at] stanford.edu)

Damon Runyon Fellow
Stanford University School of Medicine
Nachury Lab (http://openwetware.org/wiki/Nachury )


Cover

 

Stinson, B.M., Nager, A.R., Glynn, S.E., Schmitz, K.R., Baker, T.A. & Sauer, R.T. (2013) Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine. Cell 153(3): 628-39.

Wohlever ML, Nager AR, Baker TA . & Sauer, RT (2013) Engineering fluorescent protein substrates for the AAA+ Lon Protease . Protein Eng Des Sei - Epub 2013. January 28. PMID 23359718.

Glynn, S.E., Nager, A.R. Baker, T.A. & Sauer, R.T. (2012) Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine. Nat. Struct. Mol. Biol. 19, 616-622.

Nager, A.R., Baker, T.A. & Sauer, R.T. (2011) Stepwise unfolding of a β-barrel protein by the AAA+ ClpXP protease. J. Mol. Biol. 413, 4-16 .

Glynn, S.E., Martin, A., Nager, A.R., Baker, T.A. and Sauer R.T. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell, 139, 744-756.

 

RANDALL MAULDIN

Mauldin

 

Randall Mauldin
Posdoctoral Associate (March 2010-June 2011)
and NIH Postdoctoral Fellow (July 2011- March 2012)
Email (rmauldin [at] alumni.unc.edu)

Scientist
Momenta Pharmaceuticals, Inc.

 

 

Mauldin, R.V., and Sauer R.T. (2013) Allosteric regulation of DegS protease subunits through a shared energy landscape. Nature Chemical Biology , 9, 90-96.

 

STEVEN GLYNN

 

SGlynn

 

Steven Glynn
Postdoc Associate (2005-January 2012)

Email (steven.glynn [at] stonybrook.edu)

Faculty
Stony Brook University

 

GlynnImage

 

 

Stinson, B.M., Nager, A.R., Glynn, S.E., Schmitz, K.R., Baker, T.A. & Sauer, R.T. (2013) Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine. Cell 153(3): 628-39.

Glynn, S.E., Nager, A.R., Baker, T.A. & Sauer, R.T. (2012) Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine. Nat. Struct. Mol. Biol. 19, 616-622.

Glynn, S.E., Martin, A., Nager, A.R., Baker, T.A. and Sauer R.T. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell, 139, 744-756.

 

SANTIAGO LIMA

 

SLima

 

Santiago Lima
Postdoc Associate (2008-2010)
NIH Postdoc Fellow (July 2010-December 2011)

Email (slima [at] vcu.edu)

Postdoctoral Fellow
Virginia Commonwealth University

 

LimaImage

 

Lima, S., Guo, M.S., Chaba, R., Gross, C.A. & Sauer, R.T. (2013) Dual Molecular Signals Mediate the Bacterial Response to Outer-Membrane Stress. Science 340(6134):837-41.

 

JIEJIN CHEN

 

JChen

 

Jiejin Chen
Postdoc Associate (2009-November 2011)
Email (jiejinc [at] gmail.com)

Scientist I
Millennium Pharmaceuticals, Inc.


 

chenimage

 

 

 

 

SHANKAR SUNDAR

SSundar

Shankar Sundar
Graduate Student (2006-2011)
Email (ssundar06 [at] gmail.com)

Associate Consultant
Campbell Alliance

SSundarImage

Sundar, S., Baker, T.A. & Sauer, R.T. (2012) The I domain of the AAA+ Hs1UV protease coordinates substrate binding, ATP hydrolysis, and protein degradation. Protein Science 21, 188-198.

Sundar, S., McGinness, K.E., Baker, T.A. & Sauer, R.T. (2010) Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease Hs1UV. J. Mol. Biol. 403, 420-429.

 

JUNGSAN SOHN

 

JSOHN

 

 

Jungsan "J" Sohn
NIH Postdoc Fellow (2008-2011)
Email (jsohn at jhmi.edu)


Faculty
Johns Hopkins University School of Medicine

Sohn

 

Sohn J., Grant, R.A., Sauer, R.T. (2010) Allostery is an intrinsic property of the protease domain of DegS: Implications for enzyme function and evolution J. Biol. Chem. 285: 34039-47

Sohn J., Grant, R.A., Sauer, R.T. (2009) OMP peptides activate the DegS protease by a relief of inhibition mechanism. Structure 17, 1411-21

Sohn, J. & Sauer, R.T. (2009) OMP peptides modulate the activity of Degs protease by differential binding to active and inactive conformations. Mol. Cell 33, 64-74.

Sohn, J., Grant, R.A., Sauer, R.T. (2007) Allosteric activation of DegS, a stress sensor PDZ-protease. Cell. 131 572-583.

 

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