SAUER LAB

BIOLOGY DEPARTMENT
Alumni (2015-2011)
(reverse listing - please scroll down)

HOME

 

BENJAMIN STINSON

 

Benjamin Stinson's image

 

Ben Stinson

Graduate Student (June 2010 - February 2015)
and Poitras Pre-doctoral Fellow
(September 2013-August 2014)
Visiting Scientist through March 2015

Postdoctoral Associate
Harvard Medical School
Johannes Walter Lab

benjamin_stinson [at] hms.harvard.edu

 

Benjamin Stinson's research image

 

 

Stinson, B.M., Baytshtok, V., Schmitz, K.R., Baker, T.A. & Sauer, R.T. (2015) Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nat. Struct. Mol. Biol. 22, 411–416.

Cordova, J.C, Olivares, A.O., Shin, Y., Stinson, B.M., Calmat, S., Schmitz, K.R., Aubin-Tam, M-E. Baker, T.A., Lang, M.J., and Sauer R.T. (2014) Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine. Cell 158(3): 647-58. doi: 10.1016/j.cell.2014.05.043.

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.

DOMINIK BARTHELME

Barthelme

 

Dominik Barthelme
Postdoctoral Associate
January 2011-March 2013 and April 2014-Feb. 2015

German Research Foundation Fellow

April 2013 - March 2014


Postdoctoral Research Fellow
Helmholtz-Center for Infection Research, Germany
Charpentier Lab
Dominik.Barthelme [at] helmholtz-hzi.de

 

DBarthelme

 

 

 

Barthelme, D., Jauregui, R. & Sauer, R.T. (2015) An ALS disease mutation in Cdc48/p97 impairs 20S proteasome binding and proteolytic communication. Protein Sci. (in press).

Barthelme, D., Chen, J.Z., Grabenstatter, J., Baker, T.A., and Sauer, R.T. (2014) Architecture and assembly of the archaeal Cdc48•20S proteasome. Proc. Natl. Acad. Sci. USA 111, E1687-1694.

Barthelme, D. & Sauer, R.T. (2013) Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proc. Natl. Acad. Sci. USA 110(9): 3327-32.

Barthelme, D. & Sauer, R.T. (2012) Identification of the Cdc48•20S proteasome as an ancient AAA+ proteolytic machine. Science 2012 Aug 17;337(6096):843-6. Epub 2012 July 26. PMID 22837385.

ANNA DE REGT

AnnadeRegt

Anna de Regt

Microbiology Graduate Student (June 2010 - September 2014)
Visiting Scientist (October 1, 2014-January 2015)

Fred Hutchinson Cancer Research Center
(Email aderegt [at] fredhutch.org)

deRegt

 

de Regt, A.K., Baker, T.A., & Sauer, R.T. (2015) Steric clashes with bound OMP peptides activate the DegS stress-response protease. Proc. Natl. Acad. Sci. USA 112, 3326-3331.

de Regt, A.K., Kim, S., Sohn, J., Grant, R.A., Baker, T.A., & Sauer, R.T. (2015) A conserved activation cluster is required for allosteric communication in HtrA-family proteases. Structure 23, 517-526.

de Regt, A.K., Yin, Y., Withers, T.R., Wang, X., Baker, T.A., Sauer, R.T., and Yu, H.D. (2014) Overexpression of CupB5 activates alginate overproduction in Pseudomonas aeruginosa by a novel AlgW-dependent mechanism. Mol. Micro. 93, 415-425.

JASON SELLO

JasonSello

 

Jason Sello
Martin Luther King, Jr. Visiting Associate Professor (September 2013 -
July 2014)

Faculty
Brown University
Department of Chemistry
(jason_sello [at] brown.edu)

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

Postdoctoral Scholar
University of Chicago
Gordon Center for Integrative Science
Keenan Lab
Email (wohlever[at] uchicago.edu)

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

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

Email (andrewrn [at] stanford.edu)


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)


Faculty
Stony Brook University
Email (steven.glynn [at] stonybrook.edu)

 

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)

Postdoctoral Fellow
Virginia Commonwealth University


Email (slima [at] vcu.edu)

 

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)



Faculty
Johns Hopkins University School of Medicine

Email (jsohn at jhmi.edu)

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.

 

 

The Links
Biology
Microbiology
OpenWetWare

Sauer Lab, Massachusetts Institute of Technology
77 Massachusetts Avenue, 68-571
Cambridge, MA 02139
Telephone: 617.253.6077, Fax: 617.258.0673

MIT Logo