메뉴 건너뛰기




Volumn 195, Issue 1, 2013, Pages 115-125

Characterization of a MazEF toxin-antitoxin homologue from Staphylococcus equorum

Author keywords

[No Author keywords available]

Indexed keywords

ANTITOXIN; COMPLEMENTARY DNA; MAZEF TOXIN ANTITOXIN; TOXIN; UNCLASSIFIED DRUG;

EID: 84872012787     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00400-12     Document Type: Article
Times cited : (28)

References (63)
  • 1
    • 80052196405 scopus 로고    scopus 로고
    • Diversity of bacterial type II toxin-antitoxin systems: a comprehensive search and functional analysis of novel families
    • Leplae R, Geeraerts D, Hallez R, Guglielmini J, Dréze P, Van Melderen L. 2011. Diversity of bacterial type II toxin-antitoxin systems: a comprehensive search and functional analysis of novel families. Nucleic Acids Res. 39:5513-5525.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5513-5525
    • Leplae, R.1    Geeraerts, D.2    Hallez, R.3    Guglielmini, J.4    Dréze, P.5    Van Melderen, L.6
  • 4
    • 78649649439 scopus 로고    scopus 로고
    • Toxin-antitoxin systems: why so many, what for? Curr
    • Van Melderen L. 2010. Toxin-antitoxin systems: why so many, what for? Curr. Opin. Microbiol. 13:781-785.
    • (2010) Opin. Microbiol , vol.13 , pp. 781-785
    • Melderen, V.L.1
  • 6
    • 84861347512 scopus 로고    scopus 로고
    • YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli
    • Masuda H, Tan Q, Awano N, Wu KP, Inouye M. 2012. YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli. Mol. Microbiol. 84:979-989.
    • (2012) Mol. Microbiol , vol.84 , pp. 979-989
    • Masuda, H.1    Tan, Q.2    Awano, N.3    Wu, K.P.4    Inouye, M.5
  • 8
    • 14244266086 scopus 로고    scopus 로고
    • Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • Pandey DP, Gerdes K. 2005. Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res. 33:966-976.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 966-976
    • Pandey, D.P.1    Gerdes, K.2
  • 9
    • 79953171927 scopus 로고    scopus 로고
    • Prokaryotic toxin-antitoxin systems-the role in bacterial physiology and application in molecular biology
    • Bukowski M, Rojowska A, Wladyka B. 2011. Prokaryotic toxin-antitoxin systems-the role in bacterial physiology and application in molecular biology. Acta Biochim. Pol. 58:1-9.
    • (2011) Acta Biochim. Pol. , vol.58 , pp. 1-9
    • Bukowski, M.1    Rojowska, A.2    Wladyka, B.3
  • 10
    • 79953708539 scopus 로고    scopus 로고
    • A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis
    • doi:10.1371/journal.pbio.1001033
    • Mutschler H, Gebhardt M, Shoeman RL, Meinhart A. 2011. A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis. PLoS Biol. 9:e1001033. doi:
    • (2011) PLoS Biol. , vol.9
    • Mutschler, H.1    Gebhardt, M.2    Shoeman, R.L.3    Meinhart, A.4
  • 11
    • 79953808579 scopus 로고    scopus 로고
    • YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB
    • Tan Q, Awano N, Inouye M. 2011. YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB. Mol. Microbiol. 79:109-118.
    • (2011) Mol. Microbiol , vol.79 , pp. 109-118
    • Tan, Q.1    Awano, N.2    Inouye, M.3
  • 12
    • 84855464046 scopus 로고    scopus 로고
    • A cis-antisense RNA acts in trans in Staphylococcus aureus to control translation of a human cytolytic peptide
    • Sayed N, Jousselin A, Felden B. 2012. A cis-antisense RNA acts in trans in Staphylococcus aureus to control translation of a human cytolytic peptide. Nat. Struct. Mol. Biol. 19:105-112.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 105-112
    • Sayed, N.1    Jousselin, A.2    Felden, B.3
  • 13
    • 77749292157 scopus 로고    scopus 로고
    • Proteolytic regulation of toxin-antitoxin systems by ClpPC in Staphylococcus aureus
    • Donegan NP, Thompson ET, Fu Z, Cheung AL. 2010. Proteolytic regulation of toxin-antitoxin systems by ClpPC in Staphylococcus aureus. J. Bacteriol. 192:1416-1422.
    • (2010) J. Bacteriol , vol.192 , pp. 1416-1422
    • Donegan, N.P.1    Thompson, E.T.2    Fu, Z.3    Cheung, A.L.4
  • 14
    • 65249145128 scopus 로고    scopus 로고
    • Regulation of the mazEF toxin-antitoxin module in Staphylococcus aureus and its impact on sigB expression
    • Donegan NP, Cheung AL. 2009. Regulation of the mazEF toxin-antitoxin module in Staphylococcus aureus and its impact on sigB expression. J. Bacteriol. 191:2795-2805.
    • (2009) J. Bacteriol , vol.191 , pp. 2795-2805
    • Donegan, N.P.1    Cheung, A.L.2
  • 15
    • 0035937194 scopus 로고    scopus 로고
    • The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome
    • Marianovsky I, Aizenman E, Engelberg-Kulka H, Glaser G. 2001. The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome. J. Biol. Chem. 276:5975-5984.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5975-5984
    • Marianovsky, I.1    Aizenman, E.2    Engelberg-Kulka, H.3    Glaser, G.4
  • 16
    • 37449006014 scopus 로고    scopus 로고
    • Characterization of MazFSa, an endoribonuclease from Staphylococcus aureus
    • Fu Z, Donegan NP, Memmi G, Cheung AL. 2007. Characterization of MazFSa, an endoribonuclease from Staphylococcus aureus. J. Bacteriol. 189:8871-8879.
    • (2007) J. Bacteriol , vol.189 , pp. 8871-8879
    • Fu, Z.1    Donegan, N.P.2    Memmi, G.3    Cheung, A.L.4
  • 17
    • 64049118002 scopus 로고    scopus 로고
    • Overexpression of MazFsa in Staphylococcus aureus induces bacteriostasis by selectively targeting mRNAs for cleavage
    • Fu Z, Tamber S, Memmi G, Donegan NP, Cheung AL. 2009. Overexpression of MazFsa in Staphylococcus aureus induces bacteriostasis by selectively targeting mRNAs for cleavage. J. Bacteriol. 191:2051-2059.
    • (2009) J. Bacteriol , vol.191 , pp. 2051-2059
    • Fu, Z.1    Tamber, S.2    Memmi, G.3    Donegan, N.P.4    Cheung, A.L.5
  • 19
    • 65549106453 scopus 로고    scopus 로고
    • Staphylococcus aureus MazF specifically cleaves a pentad sequence, UACAU, which is unusually abundant in the mRNA for pathogenic adhesive factor SraP
    • Zhu L, Inoue K, Yoshizumi S, Kobayashi H, Zhang Y, Ouyang M, Kato F, Sugai M, Inouye M. 2009. Staphylococcus aureus MazF specifically cleaves a pentad sequence, UACAU, which is unusually abundant in the mRNA for pathogenic adhesive factor SraP. J. Bacteriol. 191:3248-3255.
    • (2009) J. Bacteriol , vol.191 , pp. 3248-3255
    • Zhu, L.1    Inoue, K.2    Yoshizumi, S.3    Kobayashi, H.4    Zhang, Y.5    Ouyang, M.6    Kato, F.7    Sugai, M.8    Inouye, M.9
  • 21
    • 40749108545 scopus 로고    scopus 로고
    • Genetic classification and distinguishing of Staphylococcus species based on different partial gap, 16S rRNA, hsp60, rpoB, sodA, and tuf gene sequences
    • Ghebremedhin B, Layer F, König W, König B. 2008. Genetic classification and distinguishing of Staphylococcus species based on different partial gap, 16S rRNA, hsp60, rpoB, sodA, and tuf gene sequences. J. Clin. Microbiol. 46:1019-1025.
    • (2008) J. Clin. Microbiol , vol.46 , pp. 1019-1025
    • Ghebremedhin, B.1    Layer, F.2    König, W.3    König, B.4
  • 22
    • 0032947008 scopus 로고    scopus 로고
    • Phylogenetic relationships of 38 taxa of the genus Staphylococcus based on 16S rRNA gene sequence analysis
    • Takahashi T, Satoh I, Kikuchi N. 1999. Phylogenetic relationships of 38 taxa of the genus Staphylococcus based on 16S rRNA gene sequence analysis. Int. J. Syst. Bacteriol. 49:725-728.
    • (1999) Int. J. Syst. Bacteriol , vol.49 , pp. 725-728
    • Takahashi, T.1    Satoh, I.2    Kikuchi, N.3
  • 24
    • 0343238149 scopus 로고    scopus 로고
    • The macrocyclic peptide antibiotic micrococcin P(1) is secreted by the food-borne bacterium Staphylococcus equorum WS 2733 and inhibits Listeria monocytogenes on soft cheese
    • Carnio MC, Höltzel A, Rudolf M, Henle T, Jung G, Scherer S. 2000. The macrocyclic peptide antibiotic micrococcin P(1) is secreted by the food-borne bacterium Staphylococcus equorum WS 2733 and inhibits Listeria monocytogenes on soft cheese. Appl. Environ. Microbiol. 66: 2378-2384.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 2378-2384
    • Carnio, M.C.1    Höltzel, A.2    Rudolf, M.3    Henle, T.4    Jung, G.5    Scherer, S.6
  • 25
    • 0035663794 scopus 로고    scopus 로고
    • Pyridinyl polythiazole class peptide antibiotic micrococcin P1, secreted by foodborne Staphylococcus equorum WS2733, is biosynthesized nonribosomally
    • Carnio MC, Stachelhaus T, Francis KP, Scherer S. 2001. Pyridinyl polythiazole class peptide antibiotic micrococcin P1, secreted by foodborne Staphylococcus equorum WS2733, is biosynthesized nonribosomally. Eur. J. Biochem. 268:6390-6401.
    • (2001) Eur. J. Biochem , vol.268 , pp. 6390-6401
    • Carnio, M.C.1    Stachelhaus, T.2    Francis, K.P.3    Scherer, S.4
  • 26
    • 77951619556 scopus 로고    scopus 로고
    • Abundance of type I toxin-antitoxin systems in bacteria: searches for new candidates and discovery of novel families
    • Fozo EM, Makarova KS, Shabalina SA, Yutin N, Koonin EV, Storz G. 2010. Abundance of type I toxin-antitoxin systems in bacteria: searches for new candidates and discovery of novel families. Nucleic Acids Res. 38: 3743-3759.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3743-3759
    • Fozo, E.M.1    Makarova, K.S.2    Shabalina, S.A.3    Yutin, N.4    Koonin, E.V.5    Storz, G.6
  • 28
    • 34547556305 scopus 로고    scopus 로고
    • The RNAz web server: prediction of thermodynamically stable and evolutionarily conserved RNA structures
    • Gruber AR, Neuböck R, Hofacker IL, Washietl S. 2007. The RNAz web server: prediction of thermodynamically stable and evolutionarily conserved RNA structures. Nucleic Acids Res. 35:W335-W338.
    • (2007) Nucleic Acids Res. , vol.35
    • Gruber, A.R.1    Neuböck, R.2    Hofacker, I.L.3    Washietl, S.4
  • 30
    • 57249083988 scopus 로고    scopus 로고
    • IntaRNA: efficient prediction of bacterial sRNA targets incorporating target site accessibility and seed regions
    • Busch A, Richter AS, Backofen R. 2008. IntaRNA: efficient prediction of bacterial sRNA targets incorporating target site accessibility and seed regions. Bioinformatics 24:2849-2856.
    • (2008) Bioinformatics , vol.24 , pp. 2849-2856
    • Busch, A.1    Richter, A.S.2    Backofen, R.3
  • 32
    • 3142725514 scopus 로고    scopus 로고
    • The analysis of stress-induced duplex destabilization in long genomic DNA sequences
    • Benham CJ, Bi C. 2004. The analysis of stress-induced duplex destabilization in long genomic DNA sequences. J. Comput. Biol. 11:519-543.
    • (2004) J. Comput. Biol. , vol.11 , pp. 519-543
    • Benham, C.J.1    Bi, C.2
  • 33
    • 79251567076 scopus 로고    scopus 로고
    • nocoRNAc: characterization of non-coding RNAs in prokaryotes
    • doi:10.1186/1471-2105-12-40
    • Herbig A, Nieselt K. 2011. nocoRNAc: characterization of non-coding RNAs in prokaryotes. BMC Bioinformatics 12:40. doi:10.1186/1471-2105-12-40.
    • (2011) BMC Bioinformatics , vol.12 , pp. 40
    • Herbig, A.1    Nieselt, K.2
  • 34
    • 39149110856 scopus 로고    scopus 로고
    • RASTA-Bacteria: a web-based tool for identifying toxin-antitoxin loci in prokaryotes
    • doi: 10.1186/gb-2007-8-8-r155
    • Sevin EW, Barloy-Hubler F. 2007. RASTA-Bacteria: a web-based tool for identifying toxin-antitoxin loci in prokaryotes. Genome Biol. 8:R155. doi: 10.1186/gb-2007-8-8-r155.
    • (2007) Genome Biol. , vol.8
    • Sevin, E.W.1    Barloy-Hubler, F.2
  • 37
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 38
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW, Moffatt BA. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189: 113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 42
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 45
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan Oacetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera A, Herbert S, Jakob A, Vollmer W, Götz F. 2005. Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan Oacetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol. Microbiol. 55:778-787.
    • (2005) Mol. Microbiol , vol.55 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Götz, F.5
  • 46
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 47
    • 84861371009 scopus 로고    scopus 로고
    • Phylogeny of the staphylococcal major autolysin and its use in genus and species typing
    • Albrecht T, Raue S, Rosenstein R, Nieselt K, Götz F. 2012. Phylogeny of the staphylococcal major autolysin and its use in genus and species typing. J. Bacteriol. 194:2630-2636.
    • (2012) J. Bacteriol. , vol.194 , pp. 2630-2636
    • Albrecht, T.1    Raue, S.2    Rosenstein, R.3    Nieselt, K.4    Götz, F.5
  • 48
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 49
    • 0027376026 scopus 로고
    • The backbone structure of the major cold-shock protein CS7.4 4 of Escherichia coli in solution includes extensive β-sheet structure
    • Chatterjee S, Jiang W, Emerson SD, Inouye M. 1993. The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive β-sheet structure. J. Biochem. 114:663-669.
    • (1993) J. Biochem , vol.114 , pp. 663-669
    • Chatterjee, S.1    Jiang, W.2    Emerson, S.D.3    Inouye, M.4
  • 51
    • 33846966329 scopus 로고    scopus 로고
    • A new integrative reporter plasmid for Streptococcus pneumoniae
    • Halfmann A, Hakenbeck R, Brückner R. 2007. A new integrative reporter plasmid for Streptococcus pneumoniae. FEMS Microbiol. Lett. 268: 217-224.
    • (2007) FEMS Microbiol. Lett. , vol.268 , pp. 217-224
    • Halfmann, A.1    Hakenbeck, R.2    Brückner, R.3
  • 52
    • 46949090318 scopus 로고    scopus 로고
    • The mRNA interferases, MazF-mt3 and MazF-mt7 from Mycobacterium tuberculosis target unique pentad sequences in single-stranded RNA
    • Zhu L, Phadtare S, Nariya H, Ouyang M, Husson RN, Inouye M. 2008. The mRNA interferases, MazF-mt3 and MazF-mt7 from Mycobacterium tuberculosis target unique pentad sequences in single-stranded RNA. Mol. Microbiol. 69:559-569.
    • (2008) Mol. Microbiol , vol.69 , pp. 559-569
    • Zhu, L.1    Phadtare, S.2    Nariya, H.3    Ouyang, M.4    Husson, R.N.5    Inouye, M.6
  • 54
    • 77950682810 scopus 로고    scopus 로고
    • Prevalence of Fst-like toxinantitoxin systems
    • Kwong SM, Jensen SO, Firth N. 2010. Prevalence of Fst-like toxinantitoxin systems. Microbiology 156:975-977.
    • (2010) Microbiology , vol.156 , pp. 975-977
    • Kwong, S.M.1    Jensen, S.O.2    Firth, N.3
  • 55
    • 69949152647 scopus 로고    scopus 로고
    • Identification and characterization of a family of toxin-antitoxin systems related to the Enterococcus faecalis plasmid pAD1 par addiction module
    • Weaver KE, Reddy SG, Brinkman CL, Patel S, Bayles KW, Endres JL. 2009. Identification and characterization of a family of toxin-antitoxin systems related to the Enterococcus faecalis plasmid pAD1 par addiction module. Microbiology 155:2930-2940.
    • (2009) Microbiology , vol.155 , pp. 2930-2940
    • Weaver, K.E.1    Reddy, S.G.2    Brinkman, C.L.3    Patel, S.4    Bayles, K.W.5    Endres, J.L.6
  • 58
    • 0029041524 scopus 로고
    • Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA
    • Helmann JD. 1995. Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA. Nucleic Acids Res. 23: 2351-2360.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2351-2360
    • Helmann, J.D.1
  • 59
    • 0033601339 scopus 로고    scopus 로고
    • SarA, a global regulator of virulence determinants in Staphylococcus aureus, binds to a conserved motif essential for sar-dependent gene regulation
    • Chien Y-T, Manna AC, Projan SJ, Cheung AL. 1999. SarA, a global regulator of virulence determinants in Staphylococcus aureus, binds to a conserved motif essential for sar-dependent gene regulation. J. Biol. Chem. 274:37169-37176.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37169-37176
    • Chien, Y.-T.1    Manna, A.C.2    Projan, S.J.3    Cheung, A.L.4
  • 60
    • 79951616353 scopus 로고    scopus 로고
    • The chromosomal mazEF locus of Streptococcus mutans encodes a functional type II toxin-antitoxin addiction system
    • Syed MA, Koyanagi S, Sharma E, Jobin MC, Yakunin AF, Lévesque CM. 2011. The chromosomal mazEF locus of Streptococcus mutans encodes a functional type II toxin-antitoxin addiction system. J. Bacteriol. 193: 1122-1130.
    • (2011) J. Bacteriol , vol.193 , pp. 1122-1130
    • Syed, M.A.1    Koyanagi, S.2    Sharma, E.3    Jobin, M.C.4    Yakunin, A.F.5    Lévesque, C.M.6
  • 61
    • 80054759036 scopus 로고    scopus 로고
    • Regulation of growth and death in Escherichia coli by toxin-antitoxin systems
    • Yamaguchi Y, Inouye M. 2011. Regulation of growth and death in Escherichia coli by toxin-antitoxin systems. Nat. Rev. Microbiol. 9:779-790.
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 779-790
    • Yamaguchi, Y.1    Inouye, M.2
  • 62
    • 0037738520 scopus 로고    scopus 로고
    • Crystal structure of the MazE/ MazF complex: molecular bases of antidote-toxin recognition
    • Kamada K, Hanaoka F, Burley SK. 2003. Crystal structure of the MazE/ MazF complex: molecular bases of antidote-toxin recognition. Mol. Cell 11:875-884.
    • (2003) Mol. Cell , vol.11 , pp. 875-884
    • Kamada, K.1    Hanaoka, F.2    Burley, S.K.3
  • 63
    • 33644792802 scopus 로고    scopus 로고
    • Improvement in the accuracy of multiple sequence alignment program MAFFT
    • Katoh K, Kuma K, Miyata T, Toh H. 2005. Improvement in the accuracy of multiple sequence alignment program MAFFT. Genome Inform. 16(1): 22-33.
    • (2005) Genome Inform , vol.16 , Issue.1 , pp. 22-33
    • Katoh, K.1    Kuma, K.2    Miyata, T.3    Toh, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.