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| Cystal structure of an unusual thioredoxin protein with a zinc finger domain. J Biol Chem. 2007 Oct 3; Contribution of the FtsQ Transmembrane Segment to Localization to the Cell Division Site. J Bacteriol. 2007 Oct;189(20):7273-80. Epub 2007 Aug 10. PMID: 17693520 [PubMed - in process] Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility. EMBO J. 2007 Aug 8;26(15):3509-20 What lies beyond uranus? Preconceptions, ignorance, serendipity and suppressors in the search for biology's secrets. Genetics. 2007 Jun;176(2):733-40. The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal. Mol Cell. 2007 May 25;26(4):511-21. The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43. Biochemistry. 2007 Mar 20;46(11):3366-77 Role for the nonessential N terminus of FtsN in divisome assembly. J Bacteriol. 2007 Jan;189(2):646-9. Epub 2006 Oct 27. Mutants, suppressors, and wrinkled colonies: Mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly. J Bacteriol. 2006 Sep 15; Phage display extends its reach. Nat Biotechnol. 2006 Jul;24(7):793-4. Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol Microbiol. 2006 Jul;61(1):33-45. Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli. J Bacteriol. 2006 Jul;188(14):5066-76. Ribonucleotide reductases: influence of environment on synthesis and activity. Antioxid Redox Signal. 2006 May-Jun;8(5-6):773-80. In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli. Antioxid Redox Signal. 2006 May-Jun;8(5-6):735-42. regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli. EMBO J. 2006 Mar 8;25(5):1137-47. Epub 2006 Feb 16. A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18872-7. Epub 2005 Dec 15. PMID: 16357193 [PubMed - indexed for MEDLINE] Should we make a fuss? A case for social responsibility in science. Nat Biotechnol. 2005 Dec;23(12):1479-80. Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J Biol Chem. 2006 Feb 24;281(8):4911-9. Epub 2005 Nov 9. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol. 2005 Jul 12;15(13):R514-26. Review. The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Sci. 2005 Jun;14(6):1630-42. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J Bacteriol. 2005 May;187(9):2983-91. Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily. J Bacteriol. 2005 Feb;187(4):1519-22. The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J Biol Chem. 2005 Mar 25;280(12):11387-94. Epub 2005 Jan 10. Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli. Genes Dev. 2005 Jan 1;19(1):127-37. The bacterial ATPase SecA functions as a monomer in protein translocation. J Biol Chem. 2005 Mar 11;280(10):9097-105. Epub 2004 Dec 23. The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases. Res Microbiol. 2004 Oct;155(8):617-22. Review. Buddelmeijer N, Beckwith J. A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. (2004). Abstract. Paper. 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. Brandon LD,
Goehring N, Janakiraman A, Yan AW, Wu T, Beckwith J, Goldberg MB.
IcsA, a polarly localized autotransporter with an atypical signal peptide,
uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially
distributed. Ortenberg R, Beckwith J. Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities. (2003). Abstract. Paper. Schierle CF, Berkmen M, Huber D, Kumamoto C, Boyd D, Beckwith J. The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. (2003). 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 Buddelmeijer
N, Beckwith J. Assembly of cell division proteins at the E.
coli cell center. 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. 21:2354-2363 (2002). Abstract. Paper. Buddelmeijer N, Judson N, Boyd D, Mekalanos JJ, Beckwith J. YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc Natl Acad Sci U S A. 99:6316-6321 (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. Chen JC, Minev M, Beckwith J. Analysis of ftsQ Mutant Alleles in Escherichia coli: Complementation, Septal Localization, and Recruitment of Downstream Cell Division Proteins. J. Bacteriol. 184:695-705 (2002). Abstract. Paper. Tian H, Beckwith J. Genetic Screen Yields Mutations in Genes Encoding All Known Components of the Escherichia coli Signal Recognition Particle Pathway. J Bacteriol. 184:111-118. (2002). 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 U S A. 98:9551-9556 (2002). Abstract. Paper. Chen JC, Beckwith J. FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol Microbiol. 42:395-413.(2001). Abstract. Paper. Leeds JA, Boyd D, Huber DR, Sonoda GK, Luu HT, Engelman HT, Beckwith J. Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library. J. Mol. Biol. 313:181-5. (2001). Abstract. Paper. 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. 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 Beckwith J. The all purpose gene fusion. Methods Enzymol. 326:3-7. (2000). No abstract available. Leeds JA, Beckwith, J. A gene fusion method for assaying interactions of protein transmembrane segments in vivo. Methods Enzymol. 327:164-75. (2000). No abstract available. 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. Tian H, Boyd D, Beckwith J. A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery. Proc. Natl. Acad. Sci. USA. 97:4730-4735. (2000). Abstract. Paper. |
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| George Georgiou, Department
of Chemistry and Chemical Engineering, University of Texas, Austin TX. With Dr. Georgiou we are studying the details of the system for isomerizing disulfide bonds in E. coli for the purpose of engineering strains that are more efficient at expressing eukaryotic proteins with multiple disulfide bonds. Alain Chaffotte, Repliement et Modélisation de Protéines, Dépt. de Biologie Structurale et Chimie, INSTITUT PASTEUR, Paris - France. Maria Luisa Tasayco, Department of Chemistry, The City College of New York, New York, NY. Elliot Crooke, Georgetown University School of Medicine, Washington, DC. Daniel Ladant, Biochimie des Interactions macromoléculaires, Dépt. de Biologie Structurale et Chimie, INSTITUT PASTEUR, Paris - France. Tom Rapoport, Department of Cell Biology, Harvard Medical School, Boston, MA. Arne Holmgren, Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden. Kirsten
Skarstad, Department of Cell Biology, Institute for Cancer Research,
The Norwegian Radium Hospital, Oslo, Norway.
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