Ursula Jakob, Ph.D.

Professor, Molecular, Cellular, and Developmental Biology
Professor, Biological Chemistry

830 N-University, Box 1048

(734) 615-1286


Molecular, Cellular, and Developmental Biology, College of Literature, Science, and the Arts
Biological Chemistry, Medical School

Areas of Interest

Biochemical aspects of the bacterial response to heat shock.

Honors & Awards

2001 Biological Scholar, University of Michigan
2000 Burroughs Wellcome Fund Career Award in the Biomedical Sciences
1998 Sokol Postdoctoral Award

Published Articles or Reviews

NemR is a Bleach-Sensing Transcription Factor.
Gray MJ, Wholey WY, Parker BW, Kim M, Jakob U. March 2013.
J Biol Chem, 288(19):13789-98 (Abstract)

Time line of redox events in aging postmitotic cells.
Brandes N, Tienson H, Lindemann A, Vitvitsky V, Reichmann D, Banerjee R, Jakob U. March 2013.
Elife, 2:e00306 (Abstract)

The roles of conditional disorder in redox proteins.
Reichmann D, Jakob U. March 2013.
Curr Opin Struct Biol, pii: S0959-440X(13)00035-3 (Abstract)

Redox Control: A black hole for oxidized glutathione.
Winther JR, Jakob U. February 2013.
Nat Chem Biol, 9(2):69-70 (Abstract)

Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked.
Powis K, Schrul B, Tienson H, Gostimskaya I, Breker M, High S, Schuldiner M, Jakob U, Schwappach B. January 2013.
J Cell Sci. 126(Pt 2):473-83 (Abstract)

Conditional disorder in chaperone action.
Bardwell JC, Jakob U. December 2012.
Trends Biochem Sci, 37(12):517-2 (Abstract)

Quantitative in vivo redox sensors uncover oxidative stress as an early event in life.
Knoefler D, Thamsen M, Koniczek M, Niemuth NJ, Diederich AK, Jakob U. September 2012.
Mol Cell, 47(5):767-7 (Abstract)

Redox, haem and CO in enzymatic catalysis and regulation.
Ragsdale SW, Yi L, Bender G, Gupta N, Kung Y, Yan L, Stich TA, Doukov T, Leichert L, Jenkins PM, Bianchetti CM, George SJ, Cramer SP, Britt RD, Jakob U, Martens JR, Phillips GN Jr, Drennan CL. June 2012.
Biochem Soc Trans, 40(3):501-7 (Abstract)

Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae.
Wholey WY, Jakob U. March 2012.
Mol Microbiol, 83(5):981-91 (Abstract)

Order out of disorder: working cycle of an intrinsically unfolded chaperone.
Reichmann D, Xu Y, Cremers CM, Ilbert M, Mittelman R, Fitzgerald MC, Jakob U. January 2012.
Cell, 148(5):947-57 (Abstract)

Using quantitative redox proteomics to dissect the yeast redoxome.
Brandes N, Reichmann D, Tienson H, Leichert LI, Jakob U. December 2011.
J Biol Chem, 286(48):41893-903 (Abstract)

E. coli chaperones DnaK, Hsp33, and Spy inhibit bacterial functional amyloid assembly.
Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. October 2011.
Prion, 5(4) (Abstract)

Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC.
Ghosh S, Cremers CM, Jakob U, Love NG. March 2011.
Mol Microbiology, 79(6):1547-56 (Abstract)

Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans.
Kumsta C, Thamsen M, Jakob U. March 2011.
Antiox Redox Signal, 14(6):1023-37 (Abstract)

Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. March 2011.
Nat Struct Mol Biol, 18(3):262-9 (Abstract)

Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?.
Zhao F, Ilbert M, Varadan R, Cremers CM, Hoyos B, Acin-Perez R, Vinogradov V, Cowburn D, Jakob U, Hammerling U. March 2011.
Antioxid Redox Signal, 14(5):757-66 (Abstract)

The redoxome: Proteomic analysis of cellular redox networks.
Thamsen M, Jakob U. February 2011.
Curr Opin Chem Biol, 15(1):113-9 (Abstract)

Is overoxidation of peroxiredoxin physiologically significant?.
Thamsen M, Kumsta C, Li F, Jakob U. February 2011.
Antioxid Redox Signal, 14(4):725-30 (Abstract)

Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.
Cremers CM, Reichmann D, Hausmann J, Ilbert M, Jakob U. April 2010.
J Biol Chem, 285(15):11243-51 (Abstract)

Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.
Xu Y, Schmitt S, Tang L, Jakob U, Fitzgerald MC. January 2010.
Biochemistry, 49(6):1346-53 (Abstract)

Protein refolding by pH-triggered chaperone binding and release.
Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. January 2010.
Proc Natl Acad Sci U S A, 107(3):1071-6 (Abstract)

Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state.
Yi L, Jenkins PM, Leichert LI, Jakob U, Martens JR, Ragsdale SW. July 2009.
J Biol Chem. 284(31):20556-61 (Abstract)

Redox-regulated chaperones.
Kumsta C, Jakob U. June 2009.
Biochemistry, 48(22):4666-76 (Abstract)

Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli.
Barth E, Gora KV, Gebendorfer KM, Settele F, Jakob U, Winter J. May 2009.
Microbiology, 155(Pt 5):1680-9 (Abstract)

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding.
Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. May 2009.
Proc Natl Acad Sci USA, 106(14):5557-62 (Abstract)

Protein refolding by pH-triggered chaperone binding and release.
Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. January 2009.
Proc Natl Acad Sci USA, 107(3):1071-6 (Abstract)

Bleach activates a redox-regulated chaperone by oxidative protein unfolding.
Winter J, Ilbert M, Graf PC, Ozcelik D, Jakob U. November 2008.
Cell, 135(4):691-701 (Abstract)

Thiol-Based Redox Switches in Eukaryotic Proteins.
Brandes N, Schmitt S, Jakob U. November 2008.
Antioxid Redox Signal, [Epub ahead of print]. (Abstract)

Quantifying Changes in the Thiol Redox Proteome Upon Oxidative Stress in Vivo.
Leichert LI, Gehrke F, Gudiseva HV, Ilbert M, Blackwell T, Walker AK, Strahler JR, Andrews PC, Jakob U. June 2008.
Proc Nat Acad Sci, 105(24):8197-202 (Abstract)

Special issue: redox regulation of protein folding. Preface.
Herrmann JM, Jakob U. April 2008.
Biochim Biophys Acta, 1783(4):519 (Abstract)

Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins.
Brandes N, Rinck A, Leichert LI, Jakob U. November 2007.
Mol Microbiol, 66(4):901-14 (Abstract)

The redox-switch domain of Hsp33 functions as dual stress sensor.
Ilbert M, Horst J, Ahrens S, Winter J, Graf PC, Lilie H, Jakob U. June 2007.
Nat Struct Mol Biol, 14(6):556-63 (Abstract)

XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders.
Mufti AR, Burstein E, Csomos RA, Graf PCF, Wilkinson JC, Dick RD, Challa M, Son JK, Bratton SB, Su GL, Brewer GJ, Jakob U, Duckett CS. August 2006.
Mol Cell, 21(6):775-85 (Abstract)

Global Methods to Monitor the Thiol-Disulfide State of Proteins in vivo.
Leichert LI, Jakob U. May 2006.
Antioxid Redox Signal, 8(5-6):763-72 (Abstract)

CoSMoS: Conserved Sequence Motif Search in the proteome.
Liu XI, Korde N, Jakob U, Leichert LIO. January 2006.
BMC Bioinformatics, 7:37 (Abstract)

Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox Regulated Chaperone Hsp33.
Winter J, Linke K, Jatzek A, Jakob U. February 2005.
Mol Cell, 17(3):381-92 (Abstract)

Protein Thiol Modifications Visualized in vivo.
Leichert L, Jakob U. November 2004.
PloS Biology, 2(11):e333 (Abstract)

Beyond Transcription - Novel Mechanisms to Regulate Molecular Chaperone Activity.
Winter J, Jakob U. September 2004.
Critical Review in Biochemistry and Molecular Biology, 39(5-6):297-317 (Abstract)

The Crystal Structure of the Reduced Zn2+-Bound Form of the B. subtilis Hsp33 Chaperone and its Implications for the Activation Mechanism.
Janda I, Devedjiev Y, Derewenda U, Dauter Z, Bielnicki J, Cooper DR, Graf PCF, Joachimiak A, Jakob U, Derewenda Z. August 2004.
Structure, 12(10):1901-7 (Abstract)

The Zinc-dependent Redox Switch Domain of the Chaperone Hsp33 has a Novel Fold.
Won HS, Low LY, DeGuzman R, Martinez-Yamout M, Jakob U, Dyson HJ. August 2004.
J Mol Biol, 341(4):893-99 (Abstract)

Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.
Hager J, Staker B, Jakob U. May 2004.
J Bact, 186(19):6634-42 (Abstract)

Activation of the redox regulated chaperone Hsp33 by domain unfolding.
Graf PCF, Martinez-Yamout M, VanHaerents S, Lilie H, Dyson JH, Jakob U. April 2004.
J Biol Chem, 279(19):20520-38 (Abstract)

Identification of a redox regulated chaperone network. 
Hoffmann JH, Graf PCF, Linke K, Lilie H, Jakob U. January 2004.
EMBO J, 23(1):160-8 (Abstract)

Redox regulation of chaperones.
Hoffmann JH, Jakob U. January 2004.
Protein Folding Handbook. eds. Buchner, J. and Kiefhaber, T., Wiley-VCH, ISBN: 3-527-30784-2.

Thioredoxin 2, an oxidative stress induced protein, contains a high affinity zinc binding site.
Collet JF, D'Souza JC, Jakob U, Bardwell JCA. November 2003.
J Biol Chem, 278(46):45325-32 (Abstract)

The roles of the two zinc binding sites in DnaJ.
Linke K, Wolfram T, Bussemer J, Jakob U. September 2003.
J Biol Chem, 278(45):44457-66 (Abstract)

Not every disulfide lasts forever: disulfide bond formation as a redox switch.
Linke K, Jakob U. August 2003.
Antioxid Redox Signal, 5(4):425-34 (Abstract)

For a list of publications from PubMed, click HERE

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