메뉴 건너뛰기




Volumn 91, Issue SUPPL. 1, 2011, Pages

ChiZ levels modulate cell division process in mycobacteria

Author keywords

Cell division; Cell wall hydrolases; ChiZ; FtsZ; Mycobacteria

Indexed keywords

BACTERIAL ENZYME; CHIZ PROTEIN; FTSZ PROTEIN; GREEN FLUORESCENT PROTEIN; HYDROLASE; UNCLASSIFIED DRUG;

EID: 84655167689     PISSN: 14729792     EISSN: 1873281X     Source Type: Journal    
DOI: 10.1016/j.tube.2011.10.022     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 77952326903 scopus 로고    scopus 로고
    • The population dynamics and control of tuberculosis
    • C. Dye, and B.G. Williams The population dynamics and control of tuberculosis Science 328 2010 856 861
    • (2010) Science , vol.328 , pp. 856-861
    • Dye, C.1    Williams, B.G.2
  • 3
    • 35848943478 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Invasion of Macrophages: Linking Bacterial Gene Expression to Environmental Cues
    • DOI 10.1016/j.chom.2007.09.006, PII S1931312807002211
    • K.H. Rohde, R.B. Abramovitch, and D.G. Russell Mycobacterium tuberculosis invasion of macrophages: linking bacterial gene expression to environmental cues Cell Host Microbe 2 2007 352 364 (Pubitemid 350056395)
    • (2007) Cell Host and Microbe , vol.2 , Issue.5 , pp. 352-364
    • Rohde, K.H.1    Abramovitch, R.B.2    Russell, D.G.3
  • 5
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • DOI 10.1046/j.1365-2958.2002.02779.x
    • J.C. Betts, P.T. Lukey, L.C. Robb, R.A. McAdam, and K. Duncan Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling Mol Microbiology 43 2002 717 731 (Pubitemid 34597265)
    • (2002) Molecular Microbiology , vol.43 , Issue.3 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 7
    • 78349251639 scopus 로고    scopus 로고
    • Reductive stress in microbes: Implications for understanding Mycobacterium tuberculosis disease and persistence
    • A. Farhana, L. Guidry, A. Srivastava, A. Singh, M.K. Hondalus, and A.J. Steyn Reductive stress in microbes: implications for understanding Mycobacterium tuberculosis disease and persistence Adv Microb Physiol 57 2010 43 117
    • (2010) Adv Microb Physiol , vol.57 , pp. 43-117
    • Farhana, A.1    Guidry, L.2    Srivastava, A.3    Singh, A.4    Hondalus, M.K.5    Steyn, A.J.6
  • 8
    • 77950534682 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin
    • R. Gupta, M. Lavollay, J.L. Mainardi, M. Arthur, W.R. Bishai, and G. Lamichhane The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin Nat Med 16 2010 466 469
    • (2010) Nat Med , vol.16 , pp. 466-469
    • Gupta, R.1    Lavollay, M.2    Mainardi, J.L.3    Arthur, M.4    Bishai, W.R.5    Lamichhane, G.6
  • 9
    • 61349183785 scopus 로고    scopus 로고
    • Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis
    • J.E. Hugonnet, L.W. Tremblay, H.I. Boshoff, C.E. Barry 3rd, and J.S. Blanchard Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis Science 323 2009 1215 1218
    • (2009) Science , vol.323 , pp. 1215-1218
    • Hugonnet, J.E.1    Tremblay, L.W.2    Boshoff, H.I.3    Barry III, C.E.4    Blanchard, J.S.5
  • 10
    • 44949093590 scopus 로고    scopus 로고
    • The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation
    • DOI 10.1128/JB.00239-08
    • M. Lavollay, M. Arthur, M. Fourgeaud, L. Dubost, A. Marie, N. Veziris, D. Blanot, L. Gutmann, and J.L. Mainardi The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L, D-transpeptidation J Bacteriol 190 2008 4360 4366 (Pubitemid 351812884)
    • (2008) Journal of Bacteriology , vol.190 , Issue.12 , pp. 4360-4366
    • Lavollay, M.1    Arthur, M.2    Fourgeaud, M.3    Dubost, L.4    Marie, A.5    Veziris, N.6    Blanot, D.7    Gutmann, L.8    Mainardi, J.-L.9
  • 11
    • 52249094198 scopus 로고    scopus 로고
    • Microbiology. Desperately seeking new antibiotics
    • D.J. Payne Microbiology. Desperately seeking new antibiotics Science 321 2008 1644 1645
    • (2008) Science , vol.321 , pp. 1644-1645
    • Payne, D.J.1
  • 12
    • 33644763314 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis cells growing in macrophages are filamentous and deficient in FtsZ rings
    • DOI 10.1128/JB.188.5.1856-1865.2006
    • A. Chauhan, M.V. Madiraju, M. Fol, H. Lofton, E. Maloney, R. Reynolds, and M. Rajagopalan Mycobacterium tuberculosis cells growing in macrophages are filamentous and deficient in FtsZ rings J Bacteriol 188 2006 1856 1865 (Pubitemid 43346864)
    • (2006) Journal of Bacteriology , vol.188 , Issue.5 , pp. 1856-1865
    • Chauhan, A.1    Madiraju, M.V.V.S.2    Fol, M.3    Lofton, H.4    Maloney, E.5    Reynolds, R.6    Rajagopalan, M.7
  • 13
    • 18844404653 scopus 로고    scopus 로고
    • Mutations in the GTP-binding and synergy loop domains of Mycobacterium tuberculosis ftsZ compromise its function in vitro and in vivo
    • DOI 10.1016/j.bbrc.2005.03.239, PII S0006291X05007461
    • M. Rajagopalan, M.A. Atkinson, H. Lofton, A. Chauhan, and M.V. Madiraju Mutations in the GTP-binding and synergy loop domains of Mycobacterium tuberculosis ftsZ compromise its function in vitro and in vivo Biochem Biophys Res Commun 331 2005 1171 1177 (Pubitemid 40692481)
    • (2005) Biochemical and Biophysical Research Communications , vol.331 , Issue.4 , pp. 1171-1177
    • Rajagopalan, M.1    Atkinson, M.A.L.2    Lofton, H.3    Chauhan, A.4    Madiraju, M.V.5
  • 15
    • 33748661485 scopus 로고    scopus 로고
    • Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase
    • DOI 10.1111/j.1365-2958.2006.05333.x
    • A. Chauhan, H. Lofton, E. Maloney, J. Moore, M. Fol, M.V. Madiraju, and M. Rajagopalan Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase Mol Microbiol 62 2006 132 147 (Pubitemid 44386555)
    • (2006) Molecular Microbiology , vol.62 , Issue.1 , pp. 132-147
    • Chauhan, A.1    Lofton, H.2    Maloney, E.3    Moore, J.4    Fol, M.5    Madiraju, M.V.V.S.6    Rajagopalan, M.7
  • 16
    • 0037067757 scopus 로고    scopus 로고
    • Interaction between FtsZ and FtsW of Mycobacterium tuberculosis
    • DOI 10.1074/jbc.M203847200
    • P. Datta, A. Dasgupta, S. Bhakta, and J. Basu Interaction between FtsZ and FtsW of Mycobacterium tuberculosis J Biol Chem 277 2002 24983 24987 (Pubitemid 34951800)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 24983-24987
    • Datta, P.1    Dasgupta, A.2    Bhakta, S.3    Basu, J.4
  • 17
    • 33751367855 scopus 로고    scopus 로고
    • Interaction between FtsW and penicillin-binding protein 3 (PBP3) directs PBP3 to mid-cell, controls cell septation and mediates the formation of a trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria
    • DOI 10.1111/j.1365-2958.2006.05491.x
    • P. Datta, A. Dasgupta, A.K. Singh, P. Mukherjee, M. Kundu, and J. Basu Interaction between FtsW and penicillin-binding protein 3 (PBP3) directs PBP3 to mid-cell, controls cell septation and mediates the formation of a trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria Mol Microbiol 62 2006 1655 1673 (Pubitemid 44813811)
    • (2006) Molecular Microbiology , vol.62 , Issue.6 , pp. 1655-1673
    • Datta, P.1    Dasgupta, A.2    Singh, A.K.3    Mukherjee, P.4    Kundu, M.5    Basu, J.6
  • 20
    • 77649150704 scopus 로고    scopus 로고
    • Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division
    • K. Sureka, T. Hossain, P. Mukherjee, P. Chatterjee, P. Datta, M. Kundu, and J. Basu Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division PLoS One 5 2010 e8590
    • (2010) PLoS One , vol.5 , pp. 8590
    • Sureka, K.1    Hossain, T.2    Mukherjee, P.3    Chatterjee, P.4    Datta, P.5    Kundu, M.6    Basu, J.7
  • 21
    • 33845966777 scopus 로고    scopus 로고
    • GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA
    • DOI 10.1074/jbc.M607216200
    • M. Thakur, and P.K. Chakraborti GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA J Biol Chem 281 2006 40107 40113 (Pubitemid 46041815)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 40107-40113
    • Thakur, M.1    Chakraborti, P.K.2
  • 22
    • 79955088372 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis septum site determining protein, Ssd encoded by rv3660c, promotes filamentation and elicits an alternative metabolic and dormancy stress response
    • K. England, R. Crew, and R.A. Slayden Mycobacterium tuberculosis septum site determining protein, Ssd encoded by rv3660c, promotes filamentation and elicits an alternative metabolic and dormancy stress response BMC Microbiol 11 2011 79
    • (2011) BMC Microbiol , vol.11 , pp. 79
    • England, K.1    Crew, R.2    Slayden, R.A.3
  • 23
    • 77950534682 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin
    • R. Gupta, M. Lavollay, J.L. Mainardi, M. Arthur, W.R. Bishai, and G. Lamichhane The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin Nat Medicine 16 2010 466 469
    • (2010) Nat Medicine , vol.16 , pp. 466-469
    • Gupta, R.1    Lavollay, M.2    Mainardi, J.L.3    Arthur, M.4    Bishai, W.R.5    Lamichhane, G.6
  • 24
    • 40349106168 scopus 로고    scopus 로고
    • A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor
    • E.C. Hett, M.C. Chao, L.L. Deng, and E.J. Rubin A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor PLoS Pathog 4 2008 e1000001
    • (2008) PLoS Pathog , vol.4 , pp. 1000001
    • Hett, E.C.1    Chao, M.C.2    Deng, L.L.3    Rubin, E.J.4
  • 25
    • 35448989031 scopus 로고    scopus 로고
    • A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis
    • DOI 10.1111/j.1365-2958.2007.05945.x
    • E.C. Hett, M.C. Chao, A.J. Steyn, S.M. Fortune, L.L. Deng, and E.J. Rubin A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis Mol Microbiol 66 2007 658 668 (Pubitemid 47621852)
    • (2007) Molecular Microbiology , vol.66 , Issue.3 , pp. 658-668
    • Hett, E.C.1    Chao, M.C.2    Steyn, A.J.3    Fortune, S.M.4    Deng, L.L.5    Rubin, E.J.6
  • 26
    • 0036229135 scopus 로고    scopus 로고
    • Physiological consequences associated with overproduction of Mycobacterium tuberculosis FtsZ in mycobacterial hosts
    • J. Dziadek, M.V. Madiraju, S.A. Rutherford, M.A. Atkinson, and M. Rajagopalan Physiological consequences associated with overproduction of Mycobacterium tuberculosis FtsZ in mycobacterial hosts Microbiology 148 2002 961 971 (Pubitemid 34436773)
    • (2002) Microbiology , vol.148 , Issue.4 , pp. 961-971
    • Dziadek, J.1    Madiraju, M.V.V.S.2    Rutherford, S.A.3    Atkinson, M.A.L.4    Rajagopalan, M.5
  • 27
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • DOI 10.1128/JB.187.7.2233-2243.2005
    • G. Karimova, N. Dautin, and D. Ladant Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis J Bacteriol 187 2005 2233 2243 (Pubitemid 40389120)
    • (2005) Journal of Bacteriology , vol.187 , Issue.7 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 29
    • 42949164129 scopus 로고    scopus 로고
    • Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria
    • DOI 10.1099/mic.0.2007/014076-0
    • C.M. Kang, S. Nyayapathy, J.Y. Lee, J.W. Suh, and R.N. Husson Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria Microbiology 154 2008 725 735 (Pubitemid 351736287)
    • (2008) Microbiology , vol.154 , Issue.3 , pp. 725-735
    • Kang, C.-M.1    Nyayapathy, S.2    Lee, J.-Y.3    Suh, J.-W.4    Husson, R.N.5
  • 31
    • 0037166304 scopus 로고    scopus 로고
    • Macrophages inhibit Salmonella Typhimurium replication through MEK/ERK kinase and phagocyte NADPH oxidase activities
    • DOI 10.1074/jbc.M110649200
    • C.M. Rosenberger, and B.B. Finlay Macrophages inhibit Salmonella typhimurium replication through MEK/ERK kinase and phagocyte NADPH oxidase activities J Biological Chemistry 277 2002 18753 18762 (Pubitemid 34952433)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18753-18762
    • Rosenberger, C.M.1    Brett Finlay, B.2
  • 32
    • 0344851907 scopus 로고    scopus 로고
    • Kinetics of the initial rounds of cell division of Toxoplasma gondii
    • DOI 10.1645/GE-112R
    • D.B. Woodmansee Kinetics of the initial rounds of cell division of Toxoplasma gondii J Parasitol 89 2003 895 898 (Pubitemid 37443224)
    • (2003) Journal of Parasitology , vol.89 , Issue.5 , pp. 895-898
    • Woodmansee, D.B.1
  • 33
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • J.V. Holtje Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli Microbiol Mol Biol Rev 62 1998 181 203
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 34
    • 0035118119 scopus 로고    scopus 로고
    • Enzymology of elongation and constriction of the murein sacculus of Escherichia coli
    • DOI 10.1016/S0300-9084(00)01226-8
    • J.V. Holtje, and C. Heidrich Enzymology of elongation and constriction of the murein sacculus of Escherichia coli Biochimie 83 2001 103 108 (Pubitemid 32181531)
    • (2001) Biochimie , vol.83 , Issue.1 , pp. 103-108
    • Holtje, J.-V.1    Heidrich, C.2
  • 35
    • 0036843026 scopus 로고    scopus 로고
    • Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli
    • DOI 10.1128/JB.184.22.6093-6099.2002
    • C. Heidrich, A. Ursinus, J. Berger, H. Schwarz, and J.V. Holtje Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli J Bacteriol 184 2002 6093 6099 (Pubitemid 35265888)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6093-6099
    • Heidrich, C.1    Ursinus, A.2    Berger, J.3    Schwarz, H.4    Holtje, J.-V.5
  • 37
    • 0031726240 scopus 로고    scopus 로고
    • An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis
    • DOI 10.1016/S0378-1097(98)00381-4, PII S0378109798003814
    • J.A. Triccas, T. Parish, W.J. Britton, and B. Gicquel An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis FEMS Microbiol Lett 167 1998 151 156 (Pubitemid 28479754)
    • (1998) FEMS Microbiology Letters , vol.167 , Issue.2 , pp. 151-156
    • Triccas, J.A.1    Parish, T.2    Britton, W.J.3    Gicquel, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.