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Volumn 14, Issue 1, 2015, Pages 107-119

First succinyl-proteome profiling of extensively drug-resistant Mycobacterium tuberculosis revealed involvement of succinylation in cellular physiology

Author keywords

antibiotic resistance; extensively drug resistant (XDR); lysine succinylation; metabolism; multi drug resistant (MDR); posttranslational modification

Indexed keywords

ANTIBIOTIC AGENT; PROTEOME; BACTERIAL PROTEIN; SUCCINIC ACID DERIVATIVE;

EID: 84920264388     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr500859a     Document Type: Article
Times cited : (105)

References (35)
  • 1
    • 84892876508 scopus 로고    scopus 로고
    • Beyond gene expression: The impact of protein post-translational modifications in bacteria
    • Cain, J. A.; Solis, N.; Cordwell, S. J. Beyond gene expression: the impact of protein post-translational modifications in bacteria J. Proteomics 2014, 97, 265-286
    • (2014) J. Proteomics , vol.97 , pp. 265-286
    • Cain, J.A.1    Solis, N.2    Cordwell, S.J.3
  • 2
    • 78650516004 scopus 로고    scopus 로고
    • Identification of lysine succinylation as a new post-translational modification
    • Zhang, Z.; Tan, M.; Xie, Z.; Dai, L.; Chen, Y.; Zhao, Y. Identification of lysine succinylation as a new post-translational modification Nat. Chem. Biol. 2011, 7 (1) 58-63
    • (2011) Nat. Chem. Biol. , vol.7 , Issue.1 , pp. 58-63
    • Zhang, Z.1    Tan, M.2    Xie, Z.3    Dai, L.4    Chen, Y.5    Zhao, Y.6
  • 4
    • 84883307077 scopus 로고    scopus 로고
    • Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
    • Weinert, B. T.; Schölz, C.; Wagner, S. A.; Iesmantavicius, V.; Su, D.; Daniel, J. A.; Choudhary, C. Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation Cell Rep. 2013, 4 (4) 842-851
    • (2013) Cell Rep. , vol.4 , Issue.4 , pp. 842-851
    • Weinert, B.T.1    Schölz, C.2    Wagner, S.A.3    Iesmantavicius, V.4    Su, D.5    Daniel, J.A.6    Choudhary, C.7
  • 5
    • 84890673317 scopus 로고    scopus 로고
    • Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli
    • Colak, G.; Xie, Z.; Zhu, A. Y.; Dai, L.; Lu, Z.; Zhang, Y.; Wan, X.; Chen, Y.; Cha, Y. H.; Lin, H. Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli Mol. Cell. Proteomics 2013, 12 (12) 3509-3520
    • (2013) Mol. Cell. Proteomics , vol.12 , Issue.12 , pp. 3509-3520
    • Colak, G.1    Xie, Z.2    Zhu, A.Y.3    Dai, L.4    Lu, Z.5    Zhang, Y.6    Wan, X.7    Chen, Y.8    Cha, Y.H.9    Lin, H.10
  • 6
    • 84904872156 scopus 로고    scopus 로고
    • The growing landscape of lysine acetylation links metabolism and cell signalling
    • Choudhary, C.; Weinert, B. T.; Nishida, Y.; Verdin, E.; Mann, M. The growing landscape of lysine acetylation links metabolism and cell signalling Nat. Rev. Mol. Cell Biol. 2014, 15 (8) 536-550
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , Issue.8 , pp. 536-550
    • Choudhary, C.1    Weinert, B.T.2    Nishida, Y.3    Verdin, E.4    Mann, M.5
  • 10
    • 84902096166 scopus 로고    scopus 로고
    • A succinyl lysine-based photo-cross-linking peptide probe for Sirtuin 5
    • Kalesh, K. A.; Tate, E. W. A succinyl lysine-based photo-cross-linking peptide probe for Sirtuin 5 Org. Biomol. Chem. 2014, 12 (25) 4310-4313
    • (2014) Org. Biomol. Chem. , vol.12 , Issue.25 , pp. 4310-4313
    • Kalesh, K.A.1    Tate, E.W.2
  • 12
    • 84901217765 scopus 로고    scopus 로고
    • Unexpected extensive lysine acetylation in the trump-card antibiotic producer Streptomyces roseosporus revealed by proteome-wide profiling
    • Liao, G.; Xie, L.; Li, X.; Cheng, Z.; Xie, J. Unexpected extensive lysine acetylation in the trump-card antibiotic producer Streptomyces roseosporus revealed by proteome-wide profiling J. Proteomics 2014, 106, 260-269
    • (2014) J. Proteomics , vol.106 , pp. 260-269
    • Liao, G.1    Xie, L.2    Li, X.3    Cheng, Z.4    Xie, J.5
  • 13
    • 77951210479 scopus 로고    scopus 로고
    • Protein-protein interactions and selection
    • Kondo, A. Protein-protein interactions and selection FEBS J. 2010, 277 (9) 1981
    • (2010) FEBS J. , vol.277 , Issue.9 , pp. 1981
    • Kondo, A.1
  • 14
    • 67549086082 scopus 로고    scopus 로고
    • Understanding the functional roles of amino acid residues in enzyme catalysis
    • Holliday, G. L.; Mitchell, J. B.; Thornton, J. M. Understanding the functional roles of amino acid residues in enzyme catalysis J. Mol. Biol. 2009, 390 (3) 560-577
    • (2009) J. Mol. Biol. , vol.390 , Issue.3 , pp. 560-577
    • Holliday, G.L.1    Mitchell, J.B.2    Thornton, J.M.3
  • 15
    • 84864835959 scopus 로고    scopus 로고
    • Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity
    • Kim, E. Y.; Kim, W. K.; Kang, H. J.; Kim, J.-H.; Chung, S. J.; Seo, Y. S.; Park, S. G.; Lee, S. C.; Bae, K.-H. Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity J. Lipid Res. 2012, 53 (9) 1864-1876
    • (2012) J. Lipid Res. , vol.53 , Issue.9 , pp. 1864-1876
    • Kim, E.Y.1    Kim, W.K.2    Kang, H.J.3    Kim, J.-H.4    Chung, S.J.5    Seo, Y.S.6    Park, S.G.7    Lee, S.C.8    Bae, K.-H.9
  • 16
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen, Y.; Zhang, J.; Lin, Y.; Lei, Q.; Guan, K. L.; Zhao, S.; Xiong, Y. Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS EMBO Rep. 2011, 12 (6) 534-541
    • (2011) EMBO Rep. , vol.12 , Issue.6 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.6    Xiong, Y.7
  • 20
    • 0037174037 scopus 로고    scopus 로고
    • A possible role of the key enzymes of the glyoxylate and gluconeogenesis pathways for fruit-body formation of the wood-rotting basidiomycete Flammulina velutipes
    • Yoon, J.-J.; Munir, E.; Miyasou, H.; Hattori, T.; Shimada, M.; Terashita, T. A possible role of the key enzymes of the glyoxylate and gluconeogenesis pathways for fruit-body formation of the wood-rotting basidiomycete Flammulina velutipes Mycoscience 2002, 43 (4) 327-332
    • (2002) Mycoscience , vol.43 , Issue.4 , pp. 327-332
    • Yoon, J.-J.1    Munir, E.2    Miyasou, H.3    Hattori, T.4    Shimada, M.5    Terashita, T.6
  • 22
    • 20944450448 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence
    • Muñoz-Elías, E. J.; McKinney, J. D. Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence Nat. Med. 2005, 11 (6) 638-644
    • (2005) Nat. Med. , vol.11 , Issue.6 , pp. 638-644
    • Muñoz-Elías, E.J.1    McKinney, J.D.2
  • 23
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • Takayama, K.; Wang, C.; Besra, G. S. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis Clin. Microbiol. Rev. 2005, 18 (1) 81-101
    • (2005) Clin. Microbiol. Rev. , vol.18 , Issue.1 , pp. 81-101
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 24
    • 34250198660 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis FAS-II condensing enzymes: Their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development
    • Bhatt, A.; Molle, V.; Besra, G. S.; Jacobs, W. R., Jr.; Kremer, L. The Mycobacterium tuberculosis FAS-II condensing enzymes: their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development Mol. Microbiol. 2007, 64 (6) 1442-1454
    • (2007) Mol. Microbiol. , vol.64 , Issue.6 , pp. 1442-1454
    • Bhatt, A.1    Molle, V.2    Besra, G.S.3    Jacobs, W.R.4    Kremer, L.5
  • 25
    • 28344453690 scopus 로고    scopus 로고
    • GroEL1: A dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria
    • Ojha, A.; Anand, M.; Bhatt, A.; Kremer, L.; Jacobs, W. R., Jr.; Hatfull, G. F. GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria Cell 2005, 123 (5) 861-873
    • (2005) Cell , vol.123 , Issue.5 , pp. 861-873
    • Ojha, A.1    Anand, M.2    Bhatt, A.3    Kremer, L.4    Jacobs, W.R.5    Hatfull, G.F.6
  • 26
    • 2942538880 scopus 로고    scopus 로고
    • Role of KatG catalase-peroxidase in mycobacterial pathogenesis: Countering the phagocyte oxidative burst
    • Ng, V. H.; Cox, J. S.; Sousa, A. O.; MacMicking, J. D.; McKinney, J. D. Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst Mol. Microbiol. 2004, 52 (5) 1291-1302
    • (2004) Mol. Microbiol. , vol.52 , Issue.5 , pp. 1291-1302
    • Ng, V.H.1    Cox, J.S.2    Sousa, A.O.3    Macmicking, J.D.4    McKinney, J.D.5
  • 27
    • 0036717879 scopus 로고    scopus 로고
    • Effect of katG mutations on the virulence of Mycobacterium tuberculosis and the implication for transmission in humans
    • Pym, A. S.; Saint-Joanis, B.; Cole, S. T. Effect of katG mutations on the virulence of Mycobacterium tuberculosis and the implication for transmission in humans Infect. Immun. 2002, 70 (9) 4955-4960
    • (2002) Infect. Immun. , vol.70 , Issue.9 , pp. 4955-4960
    • Pym, A.S.1    Saint-Joanis, B.2    Cole, S.T.3
  • 29
    • 1642543137 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis DNA gyrase: Interaction with quinolones and correlation with antimycobacterial drug activity
    • Aubry, A.; Pan, X. S.; Fisher, L. M.; Jarlier, V.; Cambau, E. Mycobacterium tuberculosis DNA gyrase: interaction with quinolones and correlation with antimycobacterial drug activity Antimicrob Agents Chemother 2004, 48 (4) 1281-8
    • (2004) Antimicrob Agents Chemother , vol.48 , Issue.4 , pp. 1281-1288
    • Aubry, A.1    Pan, X.S.2    Fisher, L.M.3    Jarlier, V.4    Cambau, E.5
  • 31
    • 0032466234 scopus 로고    scopus 로고
    • Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update
    • Ramaswamy, S.; Musser, J. M. Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update Tuberc. Lung Dis. 1998, 79 (1) 3-29
    • (1998) Tuberc. Lung Dis. , vol.79 , Issue.1 , pp. 3-29
    • Ramaswamy, S.1    Musser, J.M.2
  • 32
    • 63549144228 scopus 로고    scopus 로고
    • Emb nucleotide polymorphisms and the role of embB306 mutations in Mycobacterium tuberculosis resistance to ethambutol
    • Srivastava, S.; Ayyagari, A.; Dhole, T. N.; Nyati, K. K.; Dwivedi, S. K. emb nucleotide polymorphisms and the role of embB306 mutations in Mycobacterium tuberculosis resistance to ethambutol Int. J. Med. Microbiol. 2009, 299 (4) 269-280
    • (2009) Int. J. Med. Microbiol. , vol.299 , Issue.4 , pp. 269-280
    • Srivastava, S.1    Ayyagari, A.2    Dhole, T.N.3    Nyati, K.K.4    Dwivedi, S.K.5
  • 33
    • 29144458981 scopus 로고    scopus 로고
    • Rv0802c Acetyltransferase from Mycobacterium tuberculosis H37Rv
    • Kovacs, L.; Csanádi, á.; Kiss, é.; Miczak, A. Rv0802c Acetyltransferase from Mycobacterium tuberculosis H37Rv Acta Microbiol. Immunol. Hung. 2005, 52 (3) 363-371
    • (2005) Acta Microbiol. Immunol. Hung. , vol.52 , Issue.3 , pp. 363-371
    • Kovacs, L.1    Csanádi, A.2    Kiss, E.3    Miczak, A.4
  • 34
    • 55949133763 scopus 로고    scopus 로고
    • Rv0802c from Mycobacterium tuberculosis: The first structure of a succinyltransferase with the GNAT fold
    • Vetting, M. W.; Errey, J. C.; Blanchard, J. S. Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 2008, 64 (11) 978-985
    • (2008) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.64 , Issue.11 , pp. 978-985
    • Vetting, M.W.1    Errey, J.C.2    Blanchard, J.S.3
  • 35
    • 68349118935 scopus 로고    scopus 로고
    • Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis
    • Gu, J.; Deng, J.-Y.; Li, R.; Wei, H.; Zhang, Z.; Zhou, Y.; Zhang, Y.; Zhang, X.-E. Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis Biochemistry (Moscow) 2009, 74 (7) 743-748
    • (2009) Biochemistry (Moscow) , vol.74 , Issue.7 , pp. 743-748
    • Gu, J.1    Deng, J.-Y.2    Li, R.3    Wei, H.4    Zhang, Z.5    Zhou, Y.6    Zhang, Y.7    Zhang, X.-E.8


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