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Volumn 26, Issue 5, 2012, Pages 515-525

Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI)

Author keywords

CDI; Contact dependent growth inhibition; CysK; tRNase activity; UPEC536

Indexed keywords

BACTERIAL PROTEIN; CDIA PROTEIN; CYSTEINE SYNTHASE; NUCLEASE; RIBONUCLEASE; UNCLASSIFIED DRUG;

EID: 84857892780     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.182345.111     Document Type: Article
Times cited : (81)

References (44)
  • 3
    • 52649136629 scopus 로고    scopus 로고
    • Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB
    • Aoki SK, Malinverni JC, Jacoby K, Thomas B, Pamma R, Trinh BN, Remers S, Webb J, Braaten BA, Silhavy TJ, et al 2008. Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB. Mol Microbiol 70: 323-340.
    • (2008) Mol Microbiol , vol.70 , pp. 323-340
    • Aoki, S.K.1    Malinverni, J.C.2    Jacoby, K.3    Thomas, B.4    Pamma, R.5    Trinh, B.N.6    Remers, S.7    Webb, J.8    Braaten, B.A.9    Silhavy, T.J.10
  • 4
    • 63049109309 scopus 로고    scopus 로고
    • Contact-dependent growth inhibition causes reversible metabolic downregulation in Escherichia coli
    • Aoki SK, Webb JS, Braaten BA, Low DA. 2009. Contact-dependent growth inhibition causes reversible metabolic downregulation in Escherichia coli. J Bacteriol 191: 1777-1786.
    • (2009) J Bacteriol , vol.191 , pp. 1777-1786
    • Aoki, S.K.1    Webb, J.S.2    Braaten, B.A.3    Low, D.A.4
  • 7
    • 0031079570 scopus 로고    scopus 로고
    • Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana
    • Bogdanova N, Hell R. 1997. Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana. Plant J 11: 251-262.
    • (1997) Plant J , vol.11 , pp. 251-262
    • Bogdanova, N.1    Hell, R.2
  • 8
    • 23644440099 scopus 로고    scopus 로고
    • Interaction of serine acetyl-transferase with O-acetylserine sulfhydrylase active site: Evidence from fluorescence spectroscopy
    • Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, Huang B, Bettati S, Mozzarelli A. 2005. Interaction of serine acetyl-transferase with O-acetylserine sulfhydrylase active site: Evidence from fluorescence spectroscopy. Protein Sci 14: 2115-2124.
    • (2005) Protein Sci , vol.14 , pp. 2115-2124
    • Campanini, B.1    Speroni, F.2    Salsi, E.3    Cook, P.F.4    Roderick, S.L.5    Huang, B.6    Bettati, S.7    Mozzarelli, A.8
  • 10
    • 80051681504 scopus 로고    scopus 로고
    • FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm
    • Chauleau M, Mora L, Serba J, de Zamaroczy M. 2011. FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm. J Biol Chem 286: 29397-29407.
    • (2011) J Biol Chem , vol.286 , pp. 29397-29407
    • Chauleau, M.1    Mora, L.2    Serba, J.3    de Zamaroczy, M.4
  • 11
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci 97: 6640-6645.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 12
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants-structural and kinetic properties of the free and bound enzymes
    • Droux M, Ruffet ML, Douce R, Job D. 1998. Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants-structural and kinetic properties of the free and bound enzymes. Eur J Biochem 255: 235-245.
    • (1998) Eur J Biochem , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.L.2    Douce, R.3    Job, D.4
  • 13
    • 33747354636 scopus 로고    scopus 로고
    • Colicin M exerts its bacterio-lytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors
    • El Ghachi M, Bouhss A, Barreteau H, Touze T, Auger G, Blanot D, Mengin-Lecreulx D. 2006. Colicin M exerts its bacterio-lytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors. J Biol Chem 281: 22761-22772.
    • (2006) J Biol Chem , vol.281 , pp. 22761-22772
    • El-Ghachi, M.1    Bouhss, A.2    Barreteau, H.3    Touze, T.4    Auger, G.5    Blanot, D.6    Mengin-Lecreulx, D.7
  • 14
    • 33947545688 scopus 로고    scopus 로고
    • Structural basis for interaction of O-acetylserine sulfhydrylase and serine ace-tyltransferase in the Arabidopsis cysteine synthase complex
    • Francois JA, Kumaran S, Jez JM. 2006. Structural basis for interaction of O-acetylserine sulfhydrylase and serine ace-tyltransferase in the Arabidopsis cysteine synthase complex. Plant Cell 18: 3647-3655.
    • (2006) Plant Cell , vol.18 , pp. 3647-3655
    • Francois, J.A.1    Kumaran, S.2    Jez, J.M.3
  • 16
    • 33845932593 scopus 로고    scopus 로고
    • Prolyl-tRNA(Pro) in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA
    • Garza-Sánchez F, Janssen BD, Hayes CS. 2006. Prolyl-tRNA(Pro) in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA. J Biol Chem 281: 34258-34268.
    • (2006) J Biol Chem , vol.281 , pp. 34258-34268
    • Garza-Sánchez, F.1    Janssen, B.D.2    Hayes, C.S.3
  • 17
    • 0242361562 scopus 로고    scopus 로고
    • Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for trans-lational quality control
    • Hayes CS, Sauer RT. 2003. Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for trans-lational quality control. Mol Cell 12: 903-911.
    • (2003) Mol Cell , vol.12 , pp. 903-911
    • Hayes, C.S.1    Sauer, R.T.2
  • 18
    • 78149443620 scopus 로고    scopus 로고
    • Bacterial contact-dependent delivery systems
    • Hayes CS, Aoki SK, Low DA. 2010. Bacterial contact-dependent delivery systems. Annu Rev Genet 44: 71-90.
    • (2010) Annu Rev Genet , vol.44 , pp. 71-90
    • Hayes, C.S.1    Aoki, S.K.2    Low, D.A.3
  • 19
    • 79953219089 scopus 로고    scopus 로고
    • Activation of colicin M by the FkpA prolyl cis-trans isom-erase/chaperone
    • Helbig S, Patzer SI, Schiene-Fischer C, Zeth K, Braun V. 2011. Activation of colicin M by the FkpA prolyl cis-trans isom-erase/chaperone. J Biol Chem 286: 6280-6290.
    • (2011) J Biol Chem , vol.286 , pp. 6280-6290
    • Helbig, S.1    Patzer, S.I.2    Schiene-Fischer, C.3    Zeth, K.4    Braun, V.5
  • 20
    • 17644423923 scopus 로고    scopus 로고
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
    • Huang B, Vetting MW, Roderick SL. 2005. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. J Bacteriol 187: 3201-3205.
    • (2005) J Bacteriol , vol.187 , pp. 3201-3205
    • Huang, B.1    Vetting, M.W.2    Roderick, S.L.3
  • 21
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • Hullmann J, Patzer SI, Romer C, Hantke K, Braun V. 2008. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol Microbiol 69: 926-937.
    • (2008) Mol Microbiol , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 23
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • Kredich NM, Becker MA, Tomkins GM. 1969. Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. J Biol Chem 244: 2428-2439.
    • (1969) J Biol Chem , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 24
    • 34248217612 scopus 로고    scopus 로고
    • Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase
    • Kumaran S, Jez JM. 2007. Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase. Biochemistry 46: 5586-5594.
    • (2007) Biochemistry , vol.46 , pp. 5586-5594
    • Kumaran, S.1    Jez, J.M.2
  • 25
    • 65649133057 scopus 로고    scopus 로고
    • Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions
    • Kumaran S, Yi H, Krishnan HB, Jez JM. 2009. Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions. J Biol Chem 284: 10268-10275.
    • (2009) J Biol Chem , vol.284 , pp. 10268-10275
    • Kumaran, S.1    Yi, H.2    Krishnan, H.B.3    Jez, J.M.4
  • 26
    • 33744518327 scopus 로고    scopus 로고
    • Engineering controllable protein degradation
    • McGinness KE, Baker TA, Sauer RT. 2006. Engineering controllable protein degradation. Mol Cell 22: 701-707.
    • (2006) Mol Cell , vol.22 , pp. 701-707
    • McGinness, K.E.1    Baker, T.A.2    Sauer, R.T.3
  • 27
    • 0032610016 scopus 로고    scopus 로고
    • Purification and characterization of serine acetyltransferase from Escherichia coli partially truncated at the C-terminal region
    • Mino K, Yamanoue T, Sakiyama T, Eisaki N, Matsuyama A, Nakanishi K. 1999. Purification and characterization of serine acetyltransferase from Escherichia coli partially truncated at the C-terminal region. Biosci Biotechnol Biochem 63: 168-179.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 168-179
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 28
    • 0034278207 scopus 로고    scopus 로고
    • Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus
    • Mino K, Hiraoka K, Imamura K, Sakiyama T, Eisaki N, Matsuyama A, Nakanishi K. 2000a. Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus. Biosci Biotechnol Biochem 64: 1874-1880.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1874-1880
    • Mino, K.1    Hiraoka, K.2    Imamura, K.3    Sakiyama, T.4    Eisaki, N.5    Matsuyama, A.6    Nakanishi, K.7
  • 29
    • 0034251888 scopus 로고    scopus 로고
    • Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics
    • Mino K, Yamanoue T, Sakiyama T, Eisaki N, Matsuyama A, Nakanishi K. 2000b. Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics. Biosci Biotechnol Biochem 64: 1628-1640.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1628-1640
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 30
    • 80052334939 scopus 로고    scopus 로고
    • Identification of functional toxin/immunity genes linked to contact-dependent growth inhibition (CDI) and rearrangement hotspot (Rhs) systems
    • 10.1371/journal.pgen.1002217
    • Poole SJ, Diner EJ, Aoki SK, Braaten BA, T'kint de Roodenbeke C, Low DA, Hayes CS. 2011. Identification of functional toxin/immunity genes linked to contact-dependent growth inhibition (CDI) and rearrangement hotspot (Rhs) systems. PLoS Genet 7: e1002217. doi: 10.1371/journal.pgen.1002217.
    • (2011) PLoS Genet , vol.7
    • Poole, S.J.1    Diner, E.J.2    Aoki, S.K.3    Braaten, B.A.4    T'kint de Roodenbeke, C.5    Low, D.A.6    Hayes, C.S.7
  • 31
    • 0025737972 scopus 로고
    • A functional pseudoknot in 16S ribosomal RNA
    • Powers T, Noller HF. 1991. A functional pseudoknot in 16S ribosomal RNA. EMBO J 10: 2203-2214.
    • (1991) EMBO J , vol.10 , pp. 2203-2214
    • Powers, T.1    Noller, H.F.2
  • 32
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • Rabeh WM, Cook PF. 2004. Structure and mechanism of O-acetylserine sulfhydrylase. J Biol Chem 279: 26803-26806.
    • (2004) J Biol Chem , vol.279 , pp. 26803-26806
    • Rabeh, W.M.1    Cook, P.F.2
  • 35
    • 79959389010 scopus 로고    scopus 로고
    • + proteases: ATP-fueled machines of protein destruction
    • + proteases: ATP-fueled machines of protein destruction. Annu Rev Biochem 80: 587-612.
    • (2011) Annu Rev Biochem , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 37
    • 0020366141 scopus 로고
    • Colicin M is an inhibitor of murein biosynthesis
    • Schaller K, Holtje JV, Braun V. 1982. Colicin M is an inhibitor of murein biosynthesis. J Bacteriol 152: 994-1000.
    • (1982) J Bacteriol , vol.152 , pp. 994-1000
    • Schaller, K.1    Holtje, J.V.2    Braun, V.3
  • 38
    • 60049091769 scopus 로고    scopus 로고
    • ESX/type VII secretion systems and their role in host-pathogen interaction
    • Simeone R, Bottai D, Brosch R. 2009. ESX/type VII secretion systems and their role in host-pathogen interaction. Curr Opin Microbiol 12: 4-10.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 4-10
    • Simeone, R.1    Bottai, D.2    Brosch, R.3
  • 39
    • 79952446159 scopus 로고    scopus 로고
    • New insights into the distribution of WXG100 protein secretion systems
    • Sutcliffe IC. 2011. New insights into the distribution of WXG100 protein secretion systems. Antonie van Leeuwen-hoek 99: 127-131.
    • (2011) Antonie Van Leeuwen-hoek , vol.99 , pp. 127-131
    • Sutcliffe, I.C.1
  • 40
    • 0027183564 scopus 로고
    • Kinetic mechanisms of the A and B isozymes of O-acetylser-ine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Tai CH, Nalabolu SR, Jacobson TM, Minter DE, Cook PF. 1993. Kinetic mechanisms of the A and B isozymes of O-acetylser-ine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants. Biochemistry 32: 6433-6442.
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 41
    • 0036848756 scopus 로고    scopus 로고
    • + ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • + ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem Biol 9: 1237-1245.
    • (2002) Chem Biol , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 43
  • 44
    • 0032061345 scopus 로고    scopus 로고
    • Complexes of serine acetyltransferase and isozymes of cysteine synthase in spinach leaves
    • Zhu X, Yamaguchi T, Masada M. 1998. Complexes of serine acetyltransferase and isozymes of cysteine synthase in spinach leaves. Biosci Biotechnol Biochem 62: 947-952.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 947-952
    • Zhu, X.1    Yamaguchi, T.2    Masada, M.3


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