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Volumn 28, Issue 13, 2009, Pages 1953-1964

How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic

Author keywords

Antibiotic; MccB; MccC7; Microcin; Ubiquitin activating enzyme

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL PROTEIN; MICROCRIN C7; PROTEIN MCCB; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 67650450156     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2009.146     Document Type: Article
Times cited : (60)

References (43)
  • 2
    • 0037697382 scopus 로고    scopus 로고
    • Conservation in the mechanism of Nedd8 activation by the human AppBpl-Uba3 heterodimer
    • Bohnsack RN, Haas AL (2003) Conservation in the mechanism of Nedd8 activation by the human AppBpl-Uba3 heterodimer. J Biol Chem 278: 26823-26830
    • (2003) J Biol Chem , vol.278 , pp. 26823-26830
    • Bohnsack, R.N.1    Haas, A.L.2
  • 4
    • 0019508071 scopus 로고
    • Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system
    • Ciechanover A, Heller H, Katz-Etzion R, Hershko A (1981) Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system. Proc Natl Acad Sci USA 78: 761-765
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 761-765
    • Ciechanover, A.1    Heller, H.2    Katz-Etzion, R.3    Hershko, A.4
  • 6
    • 34548508225 scopus 로고    scopus 로고
    • Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria
    • Duquesne S, Petit V, Peduzzi J, Rebuffat S (2007) Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J Mol Microbiol Biotechnol 13: 200-209
    • (2007) J Mol Microbiol Biotechnol , vol.13 , pp. 200-209
    • Duquesne, S.1    Petit, V.2    Peduzzi, J.3    Rebuffat, S.4
  • 7
  • 9
    • 0020479562 scopus 로고
    • The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis
    • Haas AL, Rose IA (1982) The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J Biol Chem 257: 10329-10337
    • (1982) J Biol Chem , vol.257 , pp. 10329-10337
    • Haas, A.L.1    Rose, I.A.2
  • 10
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas AL, Siepmann TJ (1997) Pathways of ubiquitin conjugation. FASEB J 11: 1257-1268
    • (1997) FASEB J , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 11
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas AL, Warms JV, Hershko A, Rose IA (1982) Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J Biol Chem 257: 2543-2548
    • (1982) J Biol Chem , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 12
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser M (2000) Evolution and function of ubiquitin-like protein-conjugation systems. Nat Cell Biol 2: E153-E157
    • (2000) Nat Cell Biol , vol.2
    • Hochstrasser, M.1
  • 13
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M (2009) Origin and function of ubiquitin-like proteins. Nature 458: 422-429
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 14
    • 33846548206 scopus 로고    scopus 로고
    • Basis for a ubiquitin-like protein thioester switch toggling E1-E2 affinity
    • Huang DT, Hunt HW, Zhuang M, Ohi MD, Holton JM, Schulman BA (2007) Basis for a ubiquitin-like protein thioester switch toggling E1-E2 affinity. Nature 445: 394-398
    • (2007) Nature , vol.445 , pp. 394-398
    • Huang, D.T.1    Hunt, H.W.2    Zhuang, M.3    Ohi, M.D.4    Holton, J.M.5    Schulman, B.A.6
  • 15
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson ES, Schwienhorst I, Dohmen RJ, Blobel G (1997) The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J 16: 5509-5519
    • (1997) EMBO J , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 16
    • 33947381827 scopus 로고    scopus 로고
    • Amino acid residues required for maturation, cell uptake, and processing of translation inhibitor microcin C
    • Kazakov T, Metlitskaya A, Severinov K (2007) Amino acid residues required for maturation, cell uptake, and processing of translation inhibitor microcin C. J Bacteriol 189: 2114-2118
    • (2007) J Bacteriol , vol.189 , pp. 2114-2118
    • Kazakov, T.1    Metlitskaya, A.2    Severinov, K.3
  • 17
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H (2001) Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414: 325-329
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 18
    • 47549111312 scopus 로고    scopus 로고
    • Structural insights into El-catalyzed ubiquitin activation and transfer to conjugating enzymes
    • Lee I, Schindelin H (2008) Structural insights into El-catalyzed ubiquitin activation and transfer to conjugating enzymes. Cell 134: 268-278
    • (2008) Cell , vol.134 , pp. 268-278
    • Lee, I.1    Schindelin, H.2
  • 19
    • 30144434909 scopus 로고    scopus 로고
    • Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis
    • Lehmann C, Begley TP, Ealick SE (2006) Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45: 11-19
    • (2006) Biochemistry , vol.45 , pp. 11-19
    • Lehmann, C.1    Begley, T.P.2    Ealick, S.E.3
  • 20
    • 0035860726 scopus 로고    scopus 로고
    • Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor
    • Leimkuhler S, Wuebbens MM, Rajagopalan KV (2001) Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J Biol Chem 276: 34695-34701
    • (2001) J Biol Chem , vol.276 , pp. 34695-34701
    • Leimkuhler, S.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 21
    • 14844291338 scopus 로고    scopus 로고
    • Structures of the SUMO El provide mechanistic insights into SUMO activation and E2 recruitment to El
    • Lois LM, Lima CD (2005) Structures of the SUMO El provide mechanistic insights into SUMO activation and E2 recruitment to El. EMBO J 24: 439-451
    • (2005) EMBO J , vol.24 , pp. 439-451
    • Lois, L.M.1    Lima, C.D.2
  • 24
    • 0036905773 scopus 로고    scopus 로고
    • Ways of assembling complex natural products on modular nonribosomal peptide synthetases
    • Mootz HD, Schwarzer D, Marahiel MA (2002) Ways of assembling complex natural products on modular nonribosomal peptide synthetases. Chembiochem 3: 490-504
    • (2002) Chembiochem , vol.3 , pp. 490-504
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 26
    • 50849105102 scopus 로고    scopus 로고
    • Investigations of the McelJ-catalyzed posttranslational modification of the microcin E492 C-terminus: Linkage of ribosomal and nonribosomal peptides to form 'trojan horse' antibiotics
    • Nolan EM, Walsh CT (2008) Investigations of the McelJ-catalyzed posttranslational modification of the microcin E492 C-terminus: linkage of ribosomal and nonribosomal peptides to form 'trojan horse' antibiotics. Biochemistry 47: 9289-9299
    • (2008) Biochemistry , vol.47 , pp. 9289-9299
    • Nolan, E.M.1    Walsh, C.T.2
  • 27
    • 0022891716 scopus 로고
    • Cloning and mapping of the genetic determinants for microcin C7 production and immunity
    • Novoa MA, Diaz-Guerra L, San Millan JL, Moreno F (1986) Cloning and mapping of the genetic determinants for microcin C7 production and immunity. J Bacteriol 168: 1384-1391
    • (1986) J Bacteriol , vol.168 , pp. 1384-1391
    • Novoa, M.A.1    Diaz-Guerra, L.2    San Millan, J.L.3    Moreno, F.4
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH (2008) Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 322: 1104-1107
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 31
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart CM, Eddins MJ (2004) Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695: 55-72
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 32
    • 0030868420 scopus 로고    scopus 로고
    • Biosynthesis and processing of the molybdenum cofactors
    • Rajagopalan KV (1997) Biosynthesis and processing of the molybdenum cofactors. Biochem Soc Trans 25: 757-761
    • (1997) Biochem Soc Trans , vol.25 , pp. 757-761
    • Rajagopalan, K.V.1
  • 33
    • 41449111223 scopus 로고    scopus 로고
    • Roush RF, Nolan EM, Lohr F, Walsh CT (2008) Maturation of an Escherichia coli ribosomal peptide antibiotic by ATP-consuming N-P bond formation in microcin C7. J Am Chem Soc 130: 3603-3609
    • Roush RF, Nolan EM, Lohr F, Walsh CT (2008) Maturation of an Escherichia coli ribosomal peptide antibiotic by ATP-consuming N-P bond formation in microcin C7. J Am Chem Soc 130: 3603-3609
  • 35
    • 2442456104 scopus 로고    scopus 로고
    • A method for simultaneous alignment of multiple protein structures
    • Shatsky M, Nussinov R, Wolfson HJ (2004) A method for simultaneous alignment of multiple protein structures. Proteins 56: 143-156
    • (2004) Proteins , vol.56 , pp. 143-156
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 39
    • 33744948323 scopus 로고    scopus 로고
    • Pleiotropic effects of ATP. Mg2 + binding in the catalytic cycle of ubiquitin-activating enzyme
    • Tokgoz Z, Bohnsack RN, Haas AL (2006) Pleiotropic effects of ATP. Mg2 + binding in the catalytic cycle of ubiquitin-activating enzyme. J Biol Chem 281: 14729-14737
    • (2006) J Biol Chem , vol.281 , pp. 14729-14737
    • Tokgoz, Z.1    Bohnsack, R.N.2    Haas, A.L.3
  • 40
  • 41
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8
    • Walden H, Podgorski MS, Schulman BA (2003b) Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8. Nature 422: 330-334
    • (2003) Nature , vol.422 , pp. 330-334
    • Walden, H.1    Podgorski, M.S.2    Schulman, B.A.3
  • 42
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1: 945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 43
    • 0035902526 scopus 로고    scopus 로고
    • Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: Identification of an acyldisulfide-linked protein - protein conjugate that is functionally analogous to the ubiquitin/El complex
    • Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP (2001) Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein - protein conjugate that is functionally analogous to the ubiquitin/El complex. Proc Natl Acad Sci USA 98: 8513-8518
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8513-8518
    • Xi, J.1    Ge, Y.2    Kinsland, C.3    McLafferty, F.W.4    Begley, T.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.