메뉴 건너뛰기




Volumn 353, Issue 4, 2005, Pages 847-858

The biosynthesis of mycolic acids in Mycobacterium tuberculosis relies on multiple specialized elongation complexes interconnected by specific protein-protein interactions

Author keywords

Fatty acids; Mycolic acids; Protein protein interactions; Tuberculosis; Yeast two hybrid

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; FAS ANTIGEN; METHYLTRANSFERASE; MYCOLIC ACID;

EID: 26844537406     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.09.016     Document Type: Article
Times cited : (61)

References (36)
  • 1
    • 0028156861 scopus 로고
    • InhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis
    • A. Banerjee, E. Dubnau, A. Quemard, V. Balasubramanian, K.S. Um, and T. Wilson inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis Science 263 1994 227 230
    • (1994) Science , vol.263 , pp. 227-230
    • Banerjee, A.1    Dubnau, E.2    Quemard, A.3    Balasubramanian, V.4    Um, K.S.5    Wilson, T.6
  • 2
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
    • A. Dessen, A. Quemard, J.S. Blanchard, W.R. Jacobs Jr, and J.C. Sacchettini Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis Science 267 1995 1638 1641
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 3
    • 0038410325 scopus 로고    scopus 로고
    • Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis
    • C. Vilcheze, H.R. Morbidoni, T.R. Weisbrod, H. Iwamoto, M. Kuo, J.C. Sacchettini, and W.R. Jacobs Jr Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis J. Bacteriol. 182 2000 4059 4067
    • (2000) J. Bacteriol. , vol.182 , pp. 4059-4067
    • Vilcheze, C.1    Morbidoni, H.R.2    Weisbrod, T.R.3    Iwamoto, H.4    Kuo, M.5    Sacchettini, J.C.6    Jacobs Jr., W.R.7
  • 4
    • 0033962136 scopus 로고    scopus 로고
    • InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II
    • H. Marrakchi, G. Laneelle, and A. Quemard InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II Microbiology 146 2000 289 296
    • (2000) Microbiology , vol.146 , pp. 289-296
    • Marrakchi, H.1    Laneelle, G.2    Quemard, A.3
  • 5
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • M. Daffe, and P. Draper The envelope layers of mycobacteria with reference to their pathogenicity Advan. Microb. Physiol. 39 1998 131 203
    • (1998) Advan. Microb. Physiol. , vol.39 , pp. 131-203
    • Daffe, M.1    Draper, P.2
  • 6
    • 0035958944 scopus 로고    scopus 로고
    • Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II
    • L. Kremer, K.M. Nampoothiri, S. Lesjean, L.G. Dover, S. Graham, and J. Betts Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II J. Biol. Chem. 276 2001 27967 27974
    • (2001) J. Biol. Chem. , vol.276 , pp. 27967-27974
    • Kremer, L.1    Nampoothiri, K.M.2    Lesjean, S.3    Dover, L.G.4    Graham, S.5    Betts, J.6
  • 7
    • 0034623067 scopus 로고    scopus 로고
    • Identification and substrate specificity of beta-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis
    • K.H. Choi, L. Kremer, G.S. Besra, and C.O. Rock Identification and substrate specificity of beta-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis J. Biol. Chem. 275 2000 28201 28207
    • (2000) J. Biol. Chem. , vol.275 , pp. 28201-28207
    • Choi, K.H.1    Kremer, L.2    Besra, G.S.3    Rock, C.O.4
  • 8
    • 0035827542 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III
    • J.N. Scarsdale, G. Kazanina, X. He, K.A. Reynolds, and H.T. Wright Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III J. Biol. Chem. 276 2001 20516 20522
    • (2001) J. Biol. Chem. , vol.276 , pp. 20516-20522
    • Scarsdale, J.N.1    Kazanina, G.2    He, X.3    Reynolds, K.A.4    Wright, H.T.5
  • 9
    • 0031733687 scopus 로고    scopus 로고
    • The mabA gene from the inhA operon of Mycobacterium tuberculosis encodes a 3-ketoacyl reductase that fails to confer isoniazid resistance
    • A. Banerjee, M. Sugantino, J.C. Sacchettini, and W.R. Jacobs Jr The mabA gene from the inhA operon of Mycobacterium tuberculosis encodes a 3-ketoacyl reductase that fails to confer isoniazid resistance Microbiology 144 1998 2697 2704
    • (1998) Microbiology , vol.144 , pp. 2697-2704
    • Banerjee, A.1    Sugantino, M.2    Sacchettini, J.C.3    Jacobs Jr., W.R.4
  • 10
    • 0035861550 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB
    • M.L. Schaeffer, G. Agnihotri, C. Volker, H. Kallender, P.J. Brennan, and J.T. Lonsdale Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB J. Biol. Chem. 276 2001 47029 47037
    • (2001) J. Biol. Chem. , vol.276 , pp. 47029-47037
    • Schaeffer, M.L.1    Agnihotri, G.2    Volker, C.3    Kallender, H.4    Brennan, P.J.5    Lonsdale, J.T.6
  • 11
    • 0036606073 scopus 로고    scopus 로고
    • Mycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis
    • L. Kremer, L.G. Dover, S. Carrere, K.M. Nampoothiri, S. Lesjean, and A.K. Brown Mycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis Biochem. J. 364 2002 423 430
    • (2002) Biochem. J. , vol.364 , pp. 423-430
    • Kremer, L.1    Dover, L.G.2    Carrere, S.3    Nampoothiri, K.M.4    Lesjean, S.5    Brown, A.K.6
  • 12
    • 0036448224 scopus 로고    scopus 로고
    • The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis
    • R.A. Slayden, and C.E. Barry 3rd The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis Tuberculosis (Edinb) 82 2002 149 160
    • (2002) Tuberculosis (Edinb) , vol.82 , pp. 149-160
    • Slayden, R.A.1    Barry III, C.E.2
  • 13
    • 0347719360 scopus 로고    scopus 로고
    • A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms
    • D. Portevin, C. De Sousa-D'Auria, C. Houssin, C. Grimaldi, M. Chami, M. Daffe, and C. Guilhot A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms Proc. Natl Acad. Sci. USA 101 2004 314 319
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 314-319
    • Portevin, D.1    De Sousa-D'Auria, C.2    Houssin, C.3    Grimaldi, C.4    Chami, M.5    Daffe, M.6    Guilhot, C.7
  • 14
    • 0037192859 scopus 로고    scopus 로고
    • Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis
    • C.C. Huang, C.V. Smith, M.S. Glickman, W.R. Jacobs Jr, and J.C. Sacchettini Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis J. Biol. Chem. 277 2002 11559 11569
    • (2002) J. Biol. Chem. , vol.277 , pp. 11559-11569
    • Huang, C.C.1    Smith, C.V.2    Glickman, M.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 15
    • 0033634971 scopus 로고    scopus 로고
    • A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis
    • M.S. Glickman, J.S. Cox, and W.R. Jacobs Jr A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis Mol. Cell. 5 2000 717 727
    • (2000) Mol. Cell. , vol.5 , pp. 717-727
    • Glickman, M.S.1    Cox, J.S.2    Jacobs Jr., W.R.3
  • 16
    • 14244260489 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis controls host innate immune activation through cyclopropane modification of a glycolipid effector molecule
    • V. Rao, N. Fujiwara, S.A. Porcelli, and M.S. Glickman Mycobacterium tuberculosis controls host innate immune activation through cyclopropane modification of a glycolipid effector molecule J. Exp. Med. 201 2005 535 543
    • (2005) J. Exp. Med. , vol.201 , pp. 535-543
    • Rao, V.1    Fujiwara, N.2    Porcelli, S.A.3    Glickman, M.S.4
  • 17
    • 0034073375 scopus 로고    scopus 로고
    • Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice
    • E. Dubnau, J. Chan, C. Raynaud, V.P. Mohan, M.A. Laneelle, and K. Yu Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice Mol. Microbiol. 36 2000 630 637
    • (2000) Mol. Microbiol. , vol.36 , pp. 630-637
    • Dubnau, E.1    Chan, J.2    Raynaud, C.3    Mohan, V.P.4    Laneelle, M.A.5    Yu, K.6
  • 18
    • 0031015320 scopus 로고    scopus 로고
    • Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl keto- and hydroxy-mycolic acids
    • E. Dubnau, M.A. Laneelle, S. Soares, A. Benichou, T. Vaz, and D. Prome Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl keto- and hydroxy-mycolic acids Mol. Microbiol. 23 1997 313 322
    • (1997) Mol. Microbiol. , vol.23 , pp. 313-322
    • Dubnau, E.1    Laneelle, M.A.2    Soares, S.3    Benichou, A.4    Vaz, T.5    Prome, D.6
  • 19
    • 0029803546 scopus 로고    scopus 로고
    • A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis
    • Y. Yuan, and C.E. Barry 3rd A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis Proc. Natl Acad. Sci. USA 93 1996 12828 12833
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12828-12833
    • Yuan, Y.1    Barry III, C.E.2
  • 20
    • 0037470224 scopus 로고    scopus 로고
    • Tracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain devoid of methoxy- and ketomycolates
    • P. Dinadayala, F. Laval, C. Raynaud, A. Lemassu, M.A. Laneelle, G. Laneelle, and M. Daffe Tracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain devoid of methoxy- and ketomycolates J. Biol. Chem. 278 2003 7310 7319
    • (2003) J. Biol. Chem. , vol.278 , pp. 7310-7319
    • Dinadayala, P.1    Laval, F.2    Raynaud, C.3    Lemassu, A.4    Laneelle, M.A.5    Laneelle, G.6    Daffe, M.7
  • 21
    • 9644257517 scopus 로고    scopus 로고
    • Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability
    • R. Veyron-Churlet, O. Guerrini, L. Mourey, M. Daffe, and D. Zerbib Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability Mol. Microbiol. 54 2004 1161 1172
    • (2004) Mol. Microbiol. , vol.54 , pp. 1161-1172
    • Veyron-Churlet, R.1    Guerrini, O.2    Mourey, L.3    Daffe, M.4    Zerbib, D.5
  • 22
    • 0036299101 scopus 로고    scopus 로고
    • Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis
    • M. Cohen-Gonsaud, S. Ducasse, F. Hoh, D. Zerbib, G. Labesse, and A. Quemard Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis J. Mol. Biol. 320 2002 249 261
    • (2002) J. Mol. Biol. , vol.320 , pp. 249-261
    • Cohen-Gonsaud, M.1    Ducasse, S.2    Hoh, F.3    Zerbib, D.4    Labesse, G.5    Quemard, A.6
  • 23
    • 0037424531 scopus 로고    scopus 로고
    • The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid
    • M.S. Glickman The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid J. Biol. Chem. 278 2003 7844 7849
    • (2003) J. Biol. Chem. , vol.278 , pp. 7844-7849
    • Glickman, M.S.1
  • 24
    • 0032516871 scopus 로고    scopus 로고
    • The biosynthesis of mycolic acids in Mycobacterium tuberculosis. Enzymatic methyl(ene) transfer to acyl carrier protein bound meromycolic acid in vitro
    • Y. Yuan, D. Mead, B.G. Schroeder, Y. Zhu, and C.E. Barry 3rd The biosynthesis of mycolic acids in Mycobacterium tuberculosis. Enzymatic methyl(ene) transfer to acyl carrier protein bound meromycolic acid in vitro J. Biol. Chem. 273 1998 21282 21290
    • (1998) J. Biol. Chem. , vol.273 , pp. 21282-21290
    • Yuan, Y.1    Mead, D.2    Schroeder, B.G.3    Zhu, Y.4    Barry III, C.E.5
  • 25
    • 0018908810 scopus 로고
    • Purification of C30-56 fatty acids from Mycobacterium tuberculosis H37Ra
    • N. Qureshi, K. Takayama, and H.K. Schnoes Purification of C30-56 fatty acids from Mycobacterium tuberculosis H37Ra J. Biol Chem. 255 1980 182 189
    • (1980) J. Biol Chem. , vol.255 , pp. 182-189
    • Qureshi, N.1    Takayama, K.2    Schnoes, H.K.3
  • 26
    • 0021288384 scopus 로고
    • Biosynthesis of C30 to C56 fatty acids by an extract of Mycobacterium tuberculosis H37Ra
    • N. Qureshi, N. Sathyamoorthy, and K. Takayama Biosynthesis of C30 to C56 fatty acids by an extract of Mycobacterium tuberculosis H37Ra J. Bacteriol. 157 1984 46 52
    • (1984) J. Bacteriol. , vol.157 , pp. 46-52
    • Qureshi, N.1    Sathyamoorthy, N.2    Takayama, K.3
  • 27
    • 4544275674 scopus 로고    scopus 로고
    • Microbial type I fatty acid synthases (FAS): Major players in a network of cellular FAS systems
    • E. Schweizer, and J. Hofmann Microbial type I fatty acid synthases (FAS): major players in a network of cellular FAS systems Microbiol. Mol. Biol. Rev. 68 2004 501 517
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 501-517
    • Schweizer, E.1    Hofmann, J.2
  • 28
    • 0035853039 scopus 로고    scopus 로고
    • Human fatty acid synthase: Role of interdomain in the formation of catalytically active synthase dimer
    • S.S. Chirala, A. Jayakumar, Z.W. Gu, and S.J. Wakil Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer Proc. Natl Acad. Sci. USA 98 2001 3104 3108
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3104-3108
    • Chirala, S.S.1    Jayakumar, A.2    Gu, Z.W.3    Wakil, S.J.4
  • 29
    • 0037411269 scopus 로고    scopus 로고
    • Structural and functional organization of the animal fatty acid synthase
    • S. Smith, A. Witkowski, and A.K. Joshi Structural and functional organization of the animal fatty acid synthase Prog. Lipid Res. 42 2003 289 317
    • (2003) Prog. Lipid Res. , vol.42 , pp. 289-317
    • Smith, S.1    Witkowski, A.2    Joshi, A.K.3
  • 30
    • 0029125339 scopus 로고
    • Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: A possible link between fatty acid and polyketide biosynthesis
    • R.G. Summers, A. Ali, B. Shen, W.A. Wessel, and C.R. Hutchinson Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: a possible link between fatty acid and polyketide biosynthesis Biochemistry 34 1995 9389 9402
    • (1995) Biochemistry , vol.34 , pp. 9389-9402
    • Summers, R.G.1    Ali, A.2    Shen, B.3    Wessel, W.A.4    Hutchinson, C.R.5
  • 31
    • 0141677776 scopus 로고    scopus 로고
    • Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: Implications for therapy
    • L.Y. Gao, F. Laval, E.H. Lawson, R.K. Groger, A. Woodruff, and J.H. Morisaki Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy Mol. Microbiol. 49 2003 1547 1563
    • (2003) Mol. Microbiol. , vol.49 , pp. 1547-1563
    • Gao, L.Y.1    Laval, F.2    Lawson, E.H.3    Groger, R.K.4    Woodruff, A.5    Morisaki, J.H.6
  • 32
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • K. Takayama, C. Wang, and G.S. Besra Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis Clin. Microbiol. Rev. 18 2005 81 101
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 81-101
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 33
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • O.A. Trivedi, P. Arora, V. Sridharan, R. Tickoo, D. Mohanty, and R.S. Gokhale Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria Nature 428 2004 441 445
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 34
    • 15744389881 scopus 로고    scopus 로고
    • The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: Identification of the carboxylation product and determination of the acyl-CoA carboxylase components
    • D. Portevin, C. de Sousa-D'Auria, H. Montrozier, C. Houssin, A. Stella, and M.A. Laneelle The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components J. Biol. Chem. 280 2005 8862 8874
    • (2005) J. Biol. Chem. , vol.280 , pp. 8862-8874
    • Portevin, D.1    De Sousa-D'Auria, C.2    Montrozier, H.3    Houssin, C.4    Stella, A.5    Laneelle, M.A.6
  • 35
    • 7244242397 scopus 로고    scopus 로고
    • Acyl-CoA carboxylases (AccD2 and AccD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis
    • R. Gande, K.J. Gibson, A.K. Brown, K. Krumbach, L.G. Dover, and H. Sahm Acyl-CoA carboxylases (AccD2 and AccD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis J. Biol. Chem. 279 2004 44847 44857
    • (2004) J. Biol. Chem. , vol.279 , pp. 44847-44857
    • Gande, R.1    Gibson, K.J.2    Brown, A.K.3    Krumbach, K.4    Dover, L.G.5    Sahm, H.6
  • 36
    • 0029160015 scopus 로고
    • Protein-protein interactions between human nuclear lamins expressed in yeast
    • Q. Ye, and H.J. Worman Protein-protein interactions between human nuclear lamins expressed in yeast Exp. Cell. Res. 219 1995 292 298
    • (1995) Exp. Cell. Res. , vol.219 , pp. 292-298
    • Ye, Q.1    Worman, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.