메뉴 건너뛰기




Volumn 85, Issue 5, 2012, Pages 996-1006

Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DSBA PROTEIN; DSBB PROTEIN; DSBC PROTEIN; PSPE PROTEIN; SULFENIC ACID; SULFUR ACID DERIVATIVE; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84865559539     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08157.x     Document Type: Article
Times cited : (21)

References (36)
  • 1
    • 0037042206 scopus 로고    scopus 로고
    • PspE (phage-shock protein E) of Escherichia coli is a rhodanese
    • Adams, H., Teertstra, W., Koster, M., and Tommassen, J. (2002) PspE (phage-shock protein E) of Escherichia coli is a rhodanese. FEBS Lett 518: 173-176.
    • (2002) FEBS Lett , vol.518 , pp. 173-176
    • Adams, H.1    Teertstra, W.2    Koster, M.3    Tommassen, J.4
  • 2
    • 0026541815 scopus 로고
    • In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product
    • Akiyama, Y., Kamitani, S., Kusukawa, N., and Ito, K. (1992) In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J Biol Chem 267: 22440-22445.
    • (1992) J Biol Chem , vol.267 , pp. 22440-22445
    • Akiyama, Y.1    Kamitani, S.2    Kusukawa, N.3    Ito, K.4
  • 3
    • 0035794534 scopus 로고    scopus 로고
    • Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA
    • Bader, M.W., Hiniker, A., Regeimbal, J., Goldstone, D., Haebel, P.W., Riemer, J., etal. (2001) Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBO J 20: 1555-1562.
    • (2001) EMBO J , vol.20 , pp. 1555-1562
    • Bader, M.W.1    Hiniker, A.2    Regeimbal, J.3    Goldstone, D.4    Haebel, P.W.5    Riemer, J.6
  • 4
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C.A., McGovern, K., and Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 6
    • 85056072751 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of PspE and GlpE, two single-domain sulfurtransferases of Escherichia coli
    • Cheng, H., Donahue, J.L., Battle, S.E., Ray, W.K., and Larson, T.J. (2008) Biochemical and genetic characterization of PspE and GlpE, two single-domain sulfurtransferases of Escherichia coli. Open Microbiol J 2: 12-28.
    • (2008) Open Microbiol J , vol.2 , pp. 12-28
    • Cheng, H.1    Donahue, J.L.2    Battle, S.E.3    Ray, W.K.4    Larson, T.J.5
  • 7
    • 84860534459 scopus 로고    scopus 로고
    • A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope
    • Cho, S.-H., Parsonage, D., Thurston, C., Dutton, R.J., Poole, L.B., Collet, J.-F., and Beckwith, J. (2012) A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope. MBio 3: e00291-e00211.
    • (2012) MBio , vol.3
    • Cho, S.-H.1    Parsonage, D.2    Thurston, C.3    Dutton, R.J.4    Poole, L.B.5    Collet, J.-F.6    Beckwith, J.7
  • 8
    • 34047225116 scopus 로고    scopus 로고
    • Common themes and variations in the rhodanese superfamily
    • Cipollone, R., Ascenzi, P., and Visca, P. (2007) Common themes and variations in the rhodanese superfamily. IUBMB Life 59: 51-59.
    • (2007) IUBMB Life , vol.59 , pp. 51-59
    • Cipollone, R.1    Ascenzi, P.2    Visca, P.3
  • 9
    • 0027446271 scopus 로고
    • Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
    • Dailey, F.E., and Berg, H.C. (1993) Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc Natl Acad Sci USA 90: 1043-1047.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1043-1047
    • Dailey, F.E.1    Berg, H.C.2
  • 10
    • 22644441730 scopus 로고    scopus 로고
    • The phage-shock-protein response
    • Darwin, A.J. (2005) The phage-shock-protein response. Mol Microbiol 57: 621-628.
    • (2005) Mol Microbiol , vol.57 , pp. 621-628
    • Darwin, A.J.1
  • 11
    • 0032167852 scopus 로고    scopus 로고
    • The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm
    • Debarbieux, L., and Beckwith, J. (1998) The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm. Proc Natl Acad Sci USA 95: 10751-10756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10751-10756
    • Debarbieux, L.1    Beckwith, J.2
  • 12
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton, R.J., Boyd, D., Berkmen, M., and Beckwith, J. (2008) Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc Natl Acad Sci USA 105: 11933-11938.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 13
    • 60849121135 scopus 로고    scopus 로고
    • Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E.coli periplasm
    • Eser, M., Masip, L., Kadokura, H., Georgiou, G., and Beckwith, J. (2009) Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E.coli periplasm. Proc Natl Acad Sci USA 106: 1572-1577.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1572-1577
    • Eser, M.1    Masip, L.2    Kadokura, H.3    Georgiou, G.4    Beckwith, J.5
  • 14
    • 77649181104 scopus 로고    scopus 로고
    • Characterization of a new periplasmic single-domain rhodanese encoded by a sulfur-regulated gene in a hyperthermophilic bacterium Aquifex aeolicus
    • Giuliani, M.-C., Jourlin-Castelli, C., Leroy, G., Hachani, A., and Giudici-Orticoni, M.T. (2010) Characterization of a new periplasmic single-domain rhodanese encoded by a sulfur-regulated gene in a hyperthermophilic bacterium Aquifex aeolicus. Biochimie 92: 388-397.
    • (2010) Biochimie , vol.92 , pp. 388-397
    • Giuliani, M.-C.1    Jourlin-Castelli, C.2    Leroy, G.3    Hachani, A.4    Giudici-Orticoni, M.T.5
  • 16
    • 33744984403 scopus 로고    scopus 로고
    • Role of the intramolecular disulfide bond in FlgI, the flagellar P-ring component of Escherichia coli
    • Hizukuri, Y., Yakushi, T., Kawagishi, I., and Homma, M. (2006) Role of the intramolecular disulfide bond in FlgI, the flagellar P-ring component of Escherichia coli. J Bacteriol 188: 4190-4197.
    • (2006) J Bacteriol , vol.188 , pp. 4190-4197
    • Hizukuri, Y.1    Yakushi, T.2    Kawagishi, I.3    Homma, M.4
  • 17
    • 0028292985 scopus 로고
    • Protein folding activities of Escherichia coli protein disulfide isomerase
    • Joly, J.C., and Swartz, J.R. (1994) Protein folding activities of Escherichia coli protein disulfide isomerase. Biochemistry 33: 4231-4236.
    • (1994) Biochemistry , vol.33 , pp. 4231-4236
    • Joly, J.C.1    Swartz, J.R.2
  • 18
    • 0033564233 scopus 로고    scopus 로고
    • Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm
    • Jonda, S., Huber-Wunderlich, M., Glockshuber, R., and Mössner, E. (1999) Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm. EMBO J 18: 3271-3281.
    • (1999) EMBO J , vol.18 , pp. 3271-3281
    • Jonda, S.1    Huber-Wunderlich, M.2    Glockshuber, R.3    Mössner, E.4
  • 19
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura, H., and Beckwith, J. (2010) Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal 13: 1189-1204.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1189-1204
    • Kadokura, H.1    Beckwith, J.2
  • 20
    • 1642556877 scopus 로고    scopus 로고
    • Snapshots of DsbA in action: detection of proteins in the process of oxidative folding
    • Kadokura, H., Tian, H., Zander, T., Bardwell, J.C.A., and Beckwith, J. (2004) Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 303: 534-537.
    • (2004) Science , vol.303 , pp. 534-537
    • Kadokura, H.1    Tian, H.2    Zander, T.3    Bardwell, J.C.A.4    Beckwith, J.5
  • 21
    • 0036682611 scopus 로고    scopus 로고
    • Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
    • Katzen, F., Deshmukh, M., Daldal, F., and Beckwith, J. (2002) Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J 21: 3960-3969.
    • (2002) EMBO J , vol.21 , pp. 3960-3969
    • Katzen, F.1    Deshmukh, M.2    Daldal, F.3    Beckwith, J.4
  • 22
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • Kobayashi, T., Kishigami, S., Sone, M., Inokuchi, H., Mogi, T., and Ito, K. (1997) Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Proc Natl Acad Sci USA 94: 11857-11862.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2    Sone, M.3    Inokuchi, H.4    Mogi, T.5    Ito, K.6
  • 23
    • 79955767087 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC
    • Leverrier, P., Declercq, J.P., Denoncin, K., Vertommen, D., Hiniker, A., Cho, S.H., and Collet, J.-F. (2011) Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC. J Biol Chem 286: 16734-16742.
    • (2011) J Biol Chem , vol.286 , pp. 16734-16742
    • Leverrier, P.1    Declercq, J.P.2    Denoncin, K.3    Vertommen, D.4    Hiniker, A.5    Cho, S.H.6    Collet, J.-F.7
  • 24
    • 42049089494 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: implications for the catalytic mechanism of rhodanese
    • Li, H., Yang, F., Kang, X., Xia, B., and Jin, C. (2008) Solution structure and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: implications for the catalytic mechanism of rhodanese. Biochemistry 47: 4377-4385.
    • (2008) Biochemistry , vol.47 , pp. 4377-4385
    • Li, H.1    Yang, F.2    Kang, X.3    Xia, B.4    Jin, C.5
  • 25
  • 27
    • 40849141969 scopus 로고    scopus 로고
    • Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway
    • Pan, J.L., Sliskovic, I., and Bardwell, J.C. (2008) Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. J Mol Biol 377: 1433-1442.
    • (2008) J Mol Biol , vol.377 , pp. 1433-1442
    • Pan, J.L.1    Sliskovic, I.2    Bardwell, J.C.3
  • 28
    • 84863230655 scopus 로고    scopus 로고
    • Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase
    • Pyr Dit Ruys, S., Wang, X., Smith, E.M., Herinckx, G., Hussain, N., Rider, M.H., etal. (2012) Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase. Biochem J 442: 681-692.
    • (2012) Biochem J , vol.442 , pp. 681-692
    • Pyr Dit Ruys, S.1    Wang, X.2    Smith, E.M.3    Herinckx, G.4    Hussain, N.5    Rider, M.H.6
  • 29
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie, K.G., and Carroll, K.S. (2008) Expanding the functional diversity of proteins through cysteine oxidation. Curr Opin Chem Biol 12: 746-754.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 30
    • 79957530554 scopus 로고    scopus 로고
    • Engineered pathways for correct disulfide bond oxidation
    • Ren, G., and Bardwell, J.C.A. (2011) Engineered pathways for correct disulfide bond oxidation. Antioxid Redox Signal 14: 2399-2412.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2399-2412
    • Ren, G.1    Bardwell, J.C.A.2
  • 31
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch, A., Belin, D., Martin, N., and Beckwith, J. (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
  • 32
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., Bessette, P., Georgiou, G., and Beckwith, J. (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
  • 33
    • 79956292587 scopus 로고    scopus 로고
    • A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RcsF
    • Rogov, V.V., Rogova, N.Y., Bernhard, F., Löhr, F., and Dötsch, V. (2011) A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RcsF. J Biol Chem 286: 18775-18783.
    • (2011) J Biol Chem , vol.286 , pp. 18775-18783
    • Rogov, V.V.1    Rogova, N.Y.2    Bernhard, F.3    Löhr, F.4    Dötsch, V.5
  • 34
    • 33646205345 scopus 로고    scopus 로고
    • Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB
    • Segatori, L., Murphy, L., Arredondo, S., Kadokura, H., Gilbert, H., Beckwith, J., and Georgiou, G. (2006) Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J Biol Chem 281: 4911-4919.
    • (2006) J Biol Chem , vol.281 , pp. 4911-4919
    • Segatori, L.1    Murphy, L.2    Arredondo, S.3    Kadokura, H.4    Gilbert, H.5    Beckwith, J.6    Georgiou, G.7
  • 35
    • 72949101778 scopus 로고    scopus 로고
    • In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling
    • Shouldice, S.R., Cho, S.H., Boyd, D., Heras, B., Eser, M., Beckwith, J., etal. (2010) In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling. Mol Microbiol 75: 13-28.
    • (2010) Mol Microbiol , vol.75 , pp. 13-28
    • Shouldice, S.R.1    Cho, S.H.2    Boyd, D.3    Heras, B.4    Eser, M.5    Beckwith, J.6
  • 36
    • 0027366182 scopus 로고
    • Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH
    • Wunderlich, M., Otto, A., Seckler, R., and Glockshuber, R. (1993) Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH. Biochemistry 32: 12251-12256.
    • (1993) Biochemistry , vol.32 , pp. 12251-12256
    • Wunderlich, M.1    Otto, A.2    Seckler, R.3    Glockshuber, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.