Disulfide bonds in
protein folding
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People currently involved in this project: |
Hiroshi Kadokura, Markus Eser, Seung Hyun Cho, Melinda Faulkner, Anne-Gaëlle Planson, Rachel Dutton and Morgan Feeney |
Recent Publications:
Porat, A., Lillig, C.H., Johansson,C., Fernandes, A.P, Nilsson, L., Holmgren, A., and Beckwith, J. The reducing activity of glutaredoxin 3 towards cytoplasmic substrate proteins is restricted by methionine 43. Biochemistry 20: 3366-3377 (2007). . Cho, S.-H., and Beckwith, J. Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli. J. Bacteriol. 188:5066-76 (2006). Gon, S. and Beckwith, J. Ribonucleotide reductases : Influence of environment on synthesis and activity. Antioxidants and Redox Signalling 8:773-80 (2006). Gon, S., Faulkner, M.J, and Beckwith, J. In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of E. coli. Antioxidants and Redox Signalling 8:735-42(2006). Segatori, L., Murphy, L., Arredondo, S., Kadokura, H., Gilbert, H., Beckwith, J., and Georgiou, G. Conserved role of the linker α-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J. Biol. Chem.281:4911-9 (2006). Gon, S., Camara, J., Klungsøyr, H.K., Crooke, E., Skarstad K., and Beckwith, J. Mutations in dnaA and dnaN reveal a novel regulatory mechanism that couples deoxyribonucleotide synthesis and DNA replication during the cell cycle in E. coli. EMBO J. 25:1137-47 (2006). Sevier, C.S., Kadokura, H., Tam, V.C., Beckwith, J., Fass, D., and Kaiser, C.A. The prokaryotic enzyme DsbB may share structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Science 14:1630-1642 (2005). Huber, D., Cha, M.-I., Debarbieux, L., Planson, A.-G., López, G., Tasayco, M.L., Chaffotte, A., Beckwith, J. A selection for mutants that interfere with folding of E. coli thioredoxin-1 in vivo. Proc. Natl. Acad. Sci., U.S.A 102: 18872-18877 (2005). Kadokura, H., Nichols, L., and Beckwith, J. Mutational alterations of a key cis proline residue results in the trapping of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily. J. Bacteriol. 187:1519-1522 (2005). Berkmen, M., Boyd, D., and Beckwith, J. The non-consecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein disulfide isomerase, DsbC. J. Biol. Chem. 280:11387-94 (2005). Ortenberg R, Gon S, Porat A, Beckwith J. Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli. (2004). Abstract. Paper. Kadokura H, Tian H, Zander T, Bardwell JC, Beckwith J. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. (2004). Abstract. Paper. Katzen F, Beckwith J. Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. (2003). Abstract. Paper. Kadokura H, Katzen F, Beckwith J. Protein Disulfide Bond Formation in Prokaryotes. Annu Rev Biochem. (2003). Abstract. Paper Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex. EMBO J.21:4774-4784 (2002). Abstract. Paper. Katzen F, Deshmukh M, Daldal F, Beckwith J. Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J. 21:3960-3969 (2002). Abstract. Paper. Kadokura H, Beckwith J. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 21:2354-63 (2002). Abstract. Paper. Katzen F, Beckwith J. Disulfide bond formation in the periplasm of Escherichia coli. Methods Enzymol. 348:54-66 (2002). No abstract available. Ritz D, Beckwith J. Redox state of cytoplasmic thioredoxin. Methods Enzymol. 347:360-70 (2002). No abstract available. Ritz D, Lim J, Reynolds CM, Poole LB, Beckwith J. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Science 294:158-160. (2001). Abstract. Paper. Ritz D, Beckwith J. Roles of thiol-redox pathways in bacteria. Annu. Rev. Microbiol. 55:21-48. (2001). Abstract. Paper. Kadokura H, Beckwith J. The expanding world of oxidative protein folding. Nat Cell Biol. 3:247-249.(2001). Abstract. Paper. Goldstone D, Haebel PW, Katzen F, Bader MW, Bardwell JC, Beckwith J, Metcalf, P. DsbC activation by the N-terminal domain of DsbD. Proc. Natl. Acad. Sci. USA. 98:9551-6. (2001). Abstract. Paper. Katzen F, Beckwith J. Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade. Cell. 103:769-779. (2000). Abstract Kadokura H, Bader M, Tian H, Bardwell JC, Beckwith J. Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. Proc. Natl. Acad. Sci. USA. 97:10884-10889. (2000). Abstract. Paper. Ritz D, Patel H, Doan B, Zheng M, Åslund F, Storz G, Beckwith J. Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. J. Biol, Chem. 275:2505-2512. (2000). Abstract. Debarbieux L, Beckwith J. On the functional interchangeability, oxidant vs. reductant, of members of the thioredoxin superfamily. J. Bacteriol. 182:723-727. (2000). Abstract. Paper. Bessette PH, Åslund F, Beckwith J, Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm .Proc Natl Acad Sci U S A. 96:13703-13708. (1999). Abstract. Paper. Stewart E, Katzen F, Beckwith J. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. EMBO J. 18:5963-5971. (1999). Abstract. Paper. Debarbieux L, Beckwith J. Electron avenue: Pahtways of disulfide bond formation and isomerization. Cell. 99:117-119. (1999). Review. No abstract available. Mössner E, Huber-Wunderlich M, Rietsch A, Beckwith J, Glockshuber R, Åslund F. Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli. J. Biol. Chem. 274: 25254-25259(1999) Abstract. Paper. Åslund F, Zheng M, Beckwith J, Storz G. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci U S A. 96:6161-6165(1999) Abstract. Paper. Åslund F, Beckwith J. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell. 96:751-3 (1999). Review. No abstract available. Åslund F, Beckwith J. The thioredoxin superfamily: redundancy, specificity, and gray-area genomics. J Bacteriol. 181:1375-9 (1999). Review. Paper. Rietsch A, Beckwith J. The genetics of disulfide bond metabolism. Annu Rev Genet. 32:163-84 (1998). Review Abstract. Stewart EJ, Åslund F, Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J. 17:5543-50 (1998) Abstract. Paper. Rietsch, A., Bessette, P., Georgiou, G., and Beckwith, J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179:6601-6608 (1997). Abstract. Paper. Prinz, W.A., Åslund, F., Holmgren, A., and Beckwith, J. The role of the thioredoxin and glutaredoxin pathways in preventing disulfide bond formation in the cytoplasm. J. Biol. Chem. 272:15661-15667 (1997). Abstract. Paper. Derman, A., Prinz, W., Belin, D., and Beckwith, J. Mutants that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262:1744-1746 (1993). Abstract. Bardwell, J.C.A., McGovern, K., and Beckwith, J. Identification of a protein required for disulfide bond formation in vivo. Cell. 67:581-589 (1991). Abstract. |