메뉴 건너뛰기




Volumn 186, Issue 3, 2004, Pages 654-660

Genetic Analysis of Disulfide Isomerization in Escherichia coli: Expression of DsbC Is Modulated by RNase E-Dependent mRNA Processing

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBENZOIC ACID; BACTERIAL ENZYME; DISULFIDE; MESSENGER RNA; PROTEIN DSBC; RIBONUCLEASE; RIBONUCLEASE E; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; VARIANT OF TISSUE PLASMINOGEN ACTIVATOR;

EID: 1642581502     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.3.654-660.2004     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0026008229 scopus 로고
    • The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli
    • Babitzke, P., and S. R. Kushner. 1991. The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli. Proc. Natl. Acad. Sci. USA 88:1-5.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1-5
    • Babitzke, P.1    Kushner, S.R.2
  • 2
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette, P. H., J. J. Cotto, H. F. Gilbert, and G. Georgiou. 1999. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J. Biol. Chem. 274:7784-7792.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7784-7792
    • Bessette, P.H.1    Cotto, J.J.2    Gilbert, H.F.3    Georgiou, G.4
  • 3
    • 0035151833 scopus 로고    scopus 로고
    • Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli
    • Bessette, P. H., J. Qiu, J. C. Bardwell, J. R. Swartz, and G. Georgiou. 2001. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J. Bacteriol. 183:980-988.
    • (2001) J. Bacteriol. , vol.183 , pp. 980-988
    • Bessette, P.H.1    Qiu, J.2    Bardwell, J.C.3    Swartz, J.R.4    Georgiou, G.5
  • 4
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • Coburn, G. A., and G. A. Mackie. 1999. Degradation of mRNA in Escherichia coli: an old problem with some new twists. Prog. Nucleic Acid Res. Mol. Biol. 62:55-108.
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 5
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet, J. F., and J. C. Bardwell. 2002. Oxidative protein folding in bacteria. Mol. Microbiol. 44:1-8.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 6
    • 0036371371 scopus 로고    scopus 로고
    • Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase
    • Freedman, R. B., P. Klappa, and L. W. Ruddock. 2002. Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase. Methods Enzymol. 348:342-354.
    • (2002) Methods Enzymol. , vol.348 , pp. 342-354
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 7
    • 0028797303 scopus 로고
    • RNase E autoregulates its synthesis by controlling the degradation rate of its own mRNA in Escherichia coli: Unusual sensitivity of the rne transcript to RNase E activity
    • Jain, C., and J. G. Belasco. 1995. RNase E autoregulates its synthesis by controlling the degradation rate of its own mRNA in Escherichia coli: unusual sensitivity of the rne transcript to RNase E activity. Genes Dev. 9:84-96.
    • (1995) Genes Dev. , vol.9 , pp. 84-96
    • Jain, C.1    Belasco, J.G.2
  • 8
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen, F., and J. Beckwith. 2000. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103:769-779.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 9
    • 0029889965 scopus 로고    scopus 로고
    • RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli
    • Kido, M., K. Yamanaka, T. Mitani, H. Niki, T. Ogura, and S. Hiraga. 1996. RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli. J. Bacteriol. 178:3917-3925.
    • (1996) J. Bacteriol. , vol.178 , pp. 3917-3925
    • Kido, M.1    Yamanaka, K.2    Mitani, T.3    Niki, H.4    Ogura, T.5    Hiraga, S.6
  • 10
    • 0043224223 scopus 로고    scopus 로고
    • RraA: A protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli
    • Lee, K., X. Zhan, J. Gao, J. Qiu, Y. Feng, R. Meganathan, S. N. Cohen, and G. Georgiou. 2003. RraA: a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell 114:623-634.
    • (2003) Cell , vol.114 , pp. 623-634
    • Lee, K.1    Zhan, X.2    Gao, J.3    Qiu, J.4    Feng, Y.5    Meganathan, R.6    Cohen, S.N.7    Georgiou, G.8
  • 11
    • 0029962989 scopus 로고    scopus 로고
    • The N-terminal domain of the rne gene product has RNase E activity and is non-overlapping with the arginine-rich RNA-binding site
    • McDowall, K. J., and S. N. Cohen. 1996. The N-terminal domain of the rne gene product has RNase E activity and is non-overlapping with the arginine-rich RNA-binding site. J. Mol. Biol. 255:349-355.
    • (1996) J. Mol. Biol. , vol.255 , pp. 349-355
    • McDowall, K.J.1    Cohen, S.N.2
  • 13
    • 0028296940 scopus 로고
    • The Escherichia coli dshC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., C. Georgopoulos, and S. Raina. 1994. The Escherichia coli dshC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13:2013-2020.
    • (1994) EMBO J. , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 15
    • 0018964639 scopus 로고
    • Chromosomal location of a gene for chemical longevity of messenger ribonculeic acid in a temperature-sensitive mutant of Escherichia coli
    • Ono, M., and M. Kuwano. 1980. Chromosomal location of a gene for chemical longevity of messenger ribonculeic acid in a temperature-sensitive mutant of Escherichia coli. J. Bacteriol. 142:325-326.
    • (1980) J. Bacteriol. , vol.142 , pp. 325-326
    • Ono, M.1    Kuwano, M.2
  • 16
    • 15844371986 scopus 로고    scopus 로고
    • Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds
    • Ostermeier, M., K. De Sutter, and G. Georgiou. 1996. Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds. J. Biol. Chem. 271:10616-10622.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10616-10622
    • Ostermeier, M.1    De Sutter, K.2    Georgiou, G.3
  • 17
    • 0036571060 scopus 로고    scopus 로고
    • Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli
    • Ow, M. C., and S. R. Kushner. 2002. Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli. Genes Dev. 16:1102-1115.
    • (2002) Genes Dev. , vol.16 , pp. 1102-1115
    • Ow, M.C.1    Kushner, S.R.2
  • 18
    • 0031736826 scopus 로고    scopus 로고
    • Expression of active human tissue-type plasminogen activator in Escherichia coli
    • Qiu, J., J. R. Swartz, and G. Georgiou. 1998. Expression of active human tissue-type plasminogen activator in Escherichia coli. Appl. Environ. Microbiol. 64:4891-4896.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4891-4896
    • Qiu, J.1    Swartz, J.R.2    Georgiou, G.3
  • 19
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch, A., D. Belin, N. Martin, and J. Beckwith. 1996. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. USA 93:13048-13053.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13048-13053
    • Rietsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 20
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., P. Bessette, G. Georgiou, and J. Beckwith. 1997. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179:6602-6608.
    • (1997) J. Bacteriol. , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 21
    • 0034770083 scopus 로고    scopus 로고
    • Roles of thiol-redox pathways in bacteria
    • Ritz, D., and J. Beckwith. 2001. Roles of thiol-redox pathways in bacteria. Annu. Rev. Microbiol. 55:21-48.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 21-48
    • Ritz, D.1    Beckwith, J.2
  • 22
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik, V. E., G. Condemine, and J. Robert-Baudouy. 1994. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13:2007-2012.
    • (1994) EMBO J. , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 23
    • 0030929723 scopus 로고    scopus 로고
    • Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds
    • Sone, M., Y. Akiyama, and K. Ito. 1997. Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. J. Biol. Chem. 272:10349-10352.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10349-10352
    • Sone, M.1    Akiyama, Y.2    Ito, K.3
  • 24
    • 0033866222 scopus 로고    scopus 로고
    • Emerging features of mRNA decay in bacteria
    • Steege, D. A. 2000. Emerging features of mRNA decay in bacteria. RNA 6:1079-1090.
    • (2000) RNA , vol.6 , pp. 1079-1090
    • Steege, D.A.1
  • 25
    • 0028840292 scopus 로고
    • Evidence for an RNA binding region in the Escherichia coli processing endoribonuclease RNase E
    • Taraseviciene, L., G. R. Bjork, and B. E. Uhlin. 1995. Evidence for an RNA binding region in the Escherichia coli processing endoribonuclease RNase E. J. Biol. Chem. 270:26391-26398.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26391-26398
    • Taraseviciene, L.1    Bjork, G.R.2    Uhlin, B.E.3
  • 26
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang, R. F., and S. R. Kushner. 1991. Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli. Gene 100:195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2
  • 27
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun, A., D. Missiakas, S. Raina, and T. E. Creighton. 1995. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34:5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.