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Volumn 10, Issue 4, 2015, Pages

Control of morphological differentiation of Streptomyces coelicolor A3(2) by phosphorylation of mreC and pbp2

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL SPORE; DIFFERENTIATION; GENE LIBRARY; PROTEIN PHOSPHORYLATION; SPOROGENESIS; STREPTOMYCES COELICOLOR; SYNTHESIS; CYTOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; METABOLISM; PHOSPHORYLATION; TANDEM MASS SPECTROMETRY;

EID: 84957895010     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0125425     Document Type: Article
Times cited : (18)

References (66)
  • 1
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • 3292521
    • Glauner B, Holtje JV, Schwarz U (1988) The composition of the murein of Escherichia coli. J Biol Chem 263:10088-10095. PMID: 3292521
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Holtje, J.V.2    Schwarz, U.3
  • 2
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • 4568761
    • Schleifer KH, Kandler O (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 36:407-477. PMID: 4568761
    • (1972) Bacteriol Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 3
    • 0020654884 scopus 로고
    • Evolution of wall-less prokaryotes
    • 6195959
    • Maniloff J (1983) Evolution of wall-less prokaryotes. Annu Rev Microbiol 37:477-499. PMID: 6195959
    • (1983) Annu Rev Microbiol , vol.37 , pp. 477-499
    • Maniloff, J.1
  • 4
    • 84884512916 scopus 로고    scopus 로고
    • Wall teichoic acids of gram-positive bacteria
    • 24024634
    • Brown S, Santa Maria JP Jr., Walker S (2013) Wall teichoic acids of gram-positive bacteria. Annu Rev Microbiol 67:313-336. doi: 10.1146/annurev-micro-092412-155620 PMID: 24024634
    • (2013) Annu Rev Microbiol , vol.67 , pp. 313-336
    • Brown, S.1    Santa Maria, J.P.2    Walker, S.3
  • 5
    • 0014028915 scopus 로고
    • Synthesis of teichoic acids. VI. The formation of multiple wall polymers in Bacillus subtilis W-23
    • 4960203
    • Chin T, Burger MM, Glaser L (1966) Synthesis of teichoic acids. VI. The formation of multiple wall polymers in Bacillus subtilis W-23. Arch Biochem Biophys 116:358-367. PMID: 4960203
    • (1966) Arch Biochem Biophys , vol.116 , pp. 358-367
    • Chin, T.1    Burger, M.M.2    Glaser, L.3
  • 6
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • 18070068
    • Vollmer W (2008) Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol Rev 32:287-306. PMID: 18070068
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 7
    • 65649100437 scopus 로고    scopus 로고
    • Bacterial cell curvature through mechanical control of cell growth
    • 19279668
    • Cabeen MT, Charbon G, Vollmer W, Born P, Ausmees N, Weibel DB et al. (2009) Bacterial cell curvature through mechanical control of cell growth. EMBO J 28:1208-1219. doi: 10.1038/emboj.2009.61 PMID: 19279668
    • (2009) EMBO J , vol.28 , pp. 1208-1219
    • Cabeen, M.T.1    Charbon, G.2    Vollmer, W.3    Born, P.4    Ausmees, N.5    Weibel, D.B.6
  • 8
    • 84882662775 scopus 로고    scopus 로고
    • How to get (a) round: Mechanisms controlling growth and division of coccoid bacteria
    • 23949602
    • Pinho MG, Kjos M, Veening JW (2013) How to get (a) round: mechanisms controlling growth and division of coccoid bacteria. Nat Rev Microbiol 11:601-614. doi: 10.1038/nrmicro3088 PMID: 23949602
    • (2013) Nat Rev Microbiol , vol.11 , pp. 601-614
    • Pinho, M.G.1    Kjos, M.2    Veening, J.W.3
  • 9
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: In vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • 12530960
    • Carballido-Lopez R, Errington J (2003) The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev Cell 4:19-28. PMID: 12530960
    • (2003) Dev Cell , vol.4 , pp. 19-28
    • Carballido-Lopez, R.1    Errington, J.2
  • 10
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • 12809607
    • Daniel RA, Errington J (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113:767-776. PMID: 12809607
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 11
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • 11544518
    • van den Ent F, Amos LA, Lowe J (2001) Prokaryotic origin of the actin cytoskeleton. Nature 413:39-44. PMID: 11544518
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 12
    • 0142250762 scopus 로고    scopus 로고
    • A dynamic bacterial cytoskeleton
    • 14573351
    • Carballido-Lopez R, Errington J (2003) A dynamic bacterial cytoskeleton. Trends Cell Biol 13:577-583. PMID: 14573351
    • (2003) Trends Cell Biol , vol.13 , pp. 577-583
    • Carballido-Lopez, R.1    Errington, J.2
  • 13
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • 15272301
    • Defeu Soufo HJ, Graumann PL (2004) Dynamic movement of actin-like proteins within bacterial cells. EMBO Rep 5:789-794. PMID: 15272301
    • (2004) EMBO Rep , vol.5 , pp. 789-794
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 14
    • 33746655349 scopus 로고    scopus 로고
    • Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus
    • 16829583
    • Kim SY, Gitai Z, Kinkhabwala A, Shapiro L, Moerner WE (2006) Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc Natl Acad Sci U S A 103:10929-10934. PMID: 16829583
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10929-10934
    • Kim, S.Y.1    Gitai, Z.2    Kinkhabwala, A.3    Shapiro, L.4    Moerner, W.E.5
  • 16
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B
    • 21636745
    • Garner EC, Bernard R, Wang W, Zhuang X, Rudner DZ, Mitchison T (2011) Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333:222-225. doi: 10.1126/science.1203285 PMID: 21636745
    • (2011) Subtilis. Science , vol.333 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 17
    • 70350139098 scopus 로고    scopus 로고
    • Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis
    • 19659933
    • Kawai Y, Asai K, Errington J (2009) Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis. Mol Microbiol 73:719-731. doi: 10.1111/j.1365-2958.2009.06805.x PMID: 19659933
    • (2009) Mol Microbiol , vol.73 , pp. 719-731
    • Kawai, Y.1    Asai, K.2    Errington, J.3
  • 18
    • 66649138900 scopus 로고    scopus 로고
    • A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB
    • 19382805
    • Bean GJ, Flickinger ST, Westler WM, McCully ME, Sept D, Weibel DB et al. (2009) A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB. Biochemistry 48:4852-4857. doi: 10.1021/bi900014d PMID: 19382805
    • (2009) Biochemistry , vol.48 , pp. 4852-4857
    • Bean, G.J.1    Flickinger, S.T.2    Westler, W.M.3    McCully, M.E.4    Sept, D.5    Weibel, D.B.6
  • 19
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • 15612918
    • Kruse T, Bork-Jensen J, Gerdes K (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol 55:78-89. PMID: 15612918
    • (2005) Mol Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 20
    • 39749184735 scopus 로고    scopus 로고
    • Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis
    • 18156271
    • Formstone A, Carballido-Lopez R, Noirot P, Errington J, Scheffers DJ (2008) Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis. J Bacteriol 190:1812-1821. PMID: 18156271
    • (2008) J Bacteriol , vol.190 , pp. 1812-1821
    • Formstone, A.1    Carballido-Lopez, R.2    Noirot, P.3    Errington, J.4    Scheffers, D.J.5
  • 21
    • 33646412602 scopus 로고    scopus 로고
    • MreB of Streptomyces coelicolor is not essential for vegetative growth but is required for the integrity of aerial hyphae and spores
    • 16677297
    • Mazza P, Noens EE, Schirner K, Grantcharova N, Mommaas AM, Koerten HK, et al. (2006) MreB of Streptomyces coelicolor is not essential for vegetative growth but is required for the integrity of aerial hyphae and spores. Mol Microbiol 60:838-852. PMID: 16677297
    • (2006) Mol Microbiol , vol.60 , pp. 838-852
    • Mazza, P.1    Noens, E.E.2    Schirner, K.3    Grantcharova, N.4    Mommaas, A.M.5    Koerten, H.K.6
  • 22
    • 55549130778 scopus 로고    scopus 로고
    • Assemblies of DivIVA mark sites for hyphal branching and can establish new zones of cell wall growth in Streptomyces coelicolor
    • 18805980
    • Hempel AM, Wang SB, Letek M, Gil JA, Flardh K (2008) Assemblies of DivIVA mark sites for hyphal branching and can establish new zones of cell wall growth in Streptomyces coelicolor. J Bacteriol 190:7579-7583. doi: 10.1128/JB.00839-08 PMID: 18805980
    • (2008) J Bacteriol , vol.190 , pp. 7579-7583
    • Hempel, A.M.1    Wang, S.B.2    Letek, M.3    Gil, J.A.4    Flardh, K.5
  • 23
    • 0141789744 scopus 로고    scopus 로고
    • Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3 (2)
    • 12950918
    • Flardh K (2003) Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3 (2). Mol Microbiol 49:1523-1536. PMID: 12950918
    • (2003) Mol Microbiol , vol.49 , pp. 1523-1536
    • Flardh, K.1
  • 24
    • 84878137161 scopus 로고    scopus 로고
    • Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth
    • 23641002
    • Fuchino K, Bagchi S, Cantlay S, Sandblad L, Wu D, Bergman J, et al. (2013) Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth. Proc Natl Acad Sci U S A 110:E1889-1897. doi: 10.1073/pnas.1305358110 PMID: 23641002
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E1889-E1897
    • Fuchino, K.1    Bagchi, S.2    Cantlay, S.3    Sandblad, L.4    Wu, D.5    Bergman, J.6
  • 25
    • 84873157559 scopus 로고    scopus 로고
    • Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth in Streptomyces
    • 23297235
    • Holmes NA, Walshaw J, Leggett RM, Thibessard A, Dalton KA, Gillespie MD, et al. (2013) Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth in Streptomyces. Proc Natl Acad Sci U S A 110:E397-406. doi: 10.1073/pnas.1210657110 PMID: 23297235
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E397-E406
    • Holmes, N.A.1    Walshaw, J.2    Leggett, R.M.3    Thibessard, A.4    Dalton, K.A.5    Gillespie, M.D.6
  • 26
    • 0033804347 scopus 로고    scopus 로고
    • Identification and characterization of the mre gene region of Streptomyces coelicolor A3 (2)
    • 10954092
    • Burger A, Sichler K, Kelemen G, Buttner M, Wohlleben W (2000) Identification and characterization of the mre gene region of Streptomyces coelicolor A3 (2). Mol Gen Genet 263:1053-1060. PMID: 10954092
    • (2000) Mol Gen Genet , vol.263 , pp. 1053-1060
    • Burger, A.1    Sichler, K.2    Kelemen, G.3    Buttner, M.4    Wohlleben, W.5
  • 27
    • 79951809110 scopus 로고    scopus 로고
    • The MreBlike protein Mbl of Streptomyces coelicolor A3 (2) depends on MreB for proper localization and contributes to spore wall synthesis
    • 21257777
    • Heichlinger A, Ammelburg M, Kleinschnitz EM, Latus A, Maldener I, Flardh K, et al. (2011) The MreBlike protein Mbl of Streptomyces coelicolor A3 (2) depends on MreB for proper localization and contributes to spore wall synthesis. J Bacteriol 193:1533-1542. doi: 10.1128/JB.01100-10 PMID: 21257777
    • (2011) J Bacteriol , vol.193 , pp. 1533-1542
    • Heichlinger, A.1    Ammelburg, M.2    Kleinschnitz, E.M.3    Latus, A.4    Maldener, I.5    Flardh, K.6
  • 28
    • 79951811588 scopus 로고    scopus 로고
    • Proteins encoded by the mre gene cluster in Streptomyces coelicolor A3 (2) cooperate in spore wall synthesis
    • 21244527
    • Kleinschnitz EM, Heichlinger A, Schirner K, Winkler J, Latus A, Maldener I, et al. (2011) Proteins encoded by the mre gene cluster in Streptomyces coelicolor A3 (2) cooperate in spore wall synthesis. Mol Microbiol 79:1367-1379. doi: 10.1111/j.1365-2958.2010.07529.x PMID: 21244527
    • (2011) Mol Microbiol , vol.79 , pp. 1367-1379
    • Kleinschnitz, E.M.1    Heichlinger, A.2    Schirner, K.3    Winkler, J.4    Latus, A.5    Maldener, I.6
  • 29
    • 84977771279 scopus 로고    scopus 로고
    • Synthesis of the spore envelope in the developmental life cycle of Streptomyces coelicolor
    • 25595023
    • Sigle S, Ladwig N, WohllebenW, Muth G (2014) Synthesis of the spore envelope in the developmental life cycle of Streptomyces coelicolor. Int J Med Microbiol. 305:183-189 doi: 10.1016/j.ijmm.2014.12. 014 PMID: 25595023
    • (2014) Int J Med Microbiol. , vol.305 , pp. 183-189
    • Sigle, S.1    Ladwig, N.2    Wohlleben, W.3    Muth, G.4
  • 30
    • 0038039713 scopus 로고    scopus 로고
    • Eukaryotic-type protein kinases in Streptomyces coelicolor: Variations on a common theme
    • 12855714
    • Petrickova K, Petricek M (2003) Eukaryotic-type protein kinases in Streptomyces coelicolor: variations on a common theme. Microbiology 149:1609-1621. PMID: 12855714
    • (2003) Microbiology , vol.149 , pp. 1609-1621
    • Petrickova, K.1    Petricek, M.2
  • 31
    • 41549096949 scopus 로고    scopus 로고
    • Expression and characterization of the Streptomyces coelicolor serine/threonine protein kinase PkaD
    • 18323658
    • Urabe H, Aoyagi N, Ogawara H, Motojima K (2008) Expression and characterization of the Streptomyces coelicolor serine/threonine protein kinase PkaD. Biosci Biotechnol Biochem 72:778-785. PMID: 18323658
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 778-785
    • Urabe, H.1    Aoyagi, N.2    Ogawara, H.3    Motojima, K.4
  • 32
    • 4344568532 scopus 로고    scopus 로고
    • Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes
    • 15256567
    • Shi L, Zhang W (2004) Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes. Microbiology 150:2247-2256. PMID: 15256567
    • (2004) Microbiology , vol.150 , pp. 2247-2256
    • Shi, L.1    Zhang, W.2
  • 33
    • 33846700754 scopus 로고    scopus 로고
    • Activation of PKR: An open and shut case?
    • 17196820
    • Cole JL (2007) Activation of PKR: an open and shut case? Trends Biochem Sci 32:57-62. PMID: 17196820
    • (2007) Trends Biochem Sci , vol.32 , pp. 57-62
    • Cole, J.L.1
  • 34
    • 79960964670 scopus 로고    scopus 로고
    • The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization
    • 21829358
    • Mir M, Asong J, Li X, Cardot J, Boons GJ, Husson RN (2011) The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization. PLoS Pathog 7:e1002182. doi: 10.1371/journal.ppat.1002182 PMID: 21829358
    • (2011) PLoS Pathog , vol.7 , pp. e1002182
    • Mir, M.1    Asong, J.2    Li, X.3    Cardot, J.4    Boons, G.J.5    Husson, R.N.6
  • 35
    • 84901336227 scopus 로고    scopus 로고
    • Interplay of the serine/threonine-kinase StkP and the paralogs DivIVA and GpsB in pneumococcal cell elongation and division
    • 24722178
    • Fleurie A, Manuse S, Zhao C, Campo N, Cluzel C, Lavergne JP, et al. (2014) Interplay of the serine/threonine-kinase StkP and the paralogs DivIVA and GpsB in pneumococcal cell elongation and division. PLoS Genet 10:e1004275. doi: 10.1371/journal.pgen. 1004275 PMID: 24722178
    • (2014) PLoS Genet , vol.10 , pp. e1004275
    • Fleurie, A.1    Manuse, S.2    Zhao, C.3    Campo, N.4    Cluzel, C.5    Lavergne, J.P.6
  • 36
    • 61349099574 scopus 로고    scopus 로고
    • The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum
    • 18974047
    • Fiuza M, Canova MJ, Patin D, Letek M, Zanella-Cleon I, Becchi M., et al. (2008) The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum. J Biol Chem 283:36553-36563. doi: 10.1074/jbc. M807175200 PMID: 18974047
    • (2008) J Biol Chem , vol.283 , pp. 36553-36563
    • Fiuza, M.1    Canova, M.J.2    Patin, D.3    Letek, M.4    Zanella-Cleon, I.5    Becchi, M.6
  • 38
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • 15752190
    • Formstone A, Errington J (2005) A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol Microbiol 55:1646-1657. PMID: 15752190
    • (2005) Mol Microbiol , vol.55 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 39
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • 12015977
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282. PMID: 12015977
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 40
    • 79952426399 scopus 로고    scopus 로고
    • Eukaryote-like serine/threonine kinases and phosphatases in bacteria
    • 21372323
    • Pereira SF, Goss L, Dworkin J (2011) Eukaryote-like serine/threonine kinases and phosphatases in bacteria. Microbiol Mol Biol Rev 75:192-212. doi: 10.1128/MMBR.00042-10 PMID: 21372323
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 192-212
    • Pereira, S.F.1    Goss, L.2    Dworkin, J.3
  • 41
    • 84899937003 scopus 로고    scopus 로고
    • Developmental biology of Streptomyces from the perspective of 100 actinobacterial genome sequences
    • 24164321
    • Chandra G, Chater KF (2014) Developmental biology of Streptomyces from the perspective of 100 actinobacterial genome sequences. FEMS Microbiol Rev 38:345-379. doi: 10.1111/1574-6976.12047 PMID: 24164321
    • (2014) FEMS Microbiol Rev , vol.38 , pp. 345-379
    • Chandra, G.1    Chater, K.F.2
  • 42
    • 84864109890 scopus 로고    scopus 로고
    • Cell division and DNA segregation in Streptomyces: How to build a septum in the middle of nowhere?
    • 22646484
    • Jakimowicz D, van Wezel GP (2012) Cell division and DNA segregation in Streptomyces: how to build a septum in the middle of nowhere? Mol Microbiol 85:393-404. doi: 10.1111/j.1365-2958.2012.08107. x PMID: 22646484
    • (2012) Mol Microbiol , vol.85 , pp. 393-404
    • Jakimowicz, D.1    Van Wezel, G.P.2
  • 43
    • 27944458298 scopus 로고    scopus 로고
    • SsgA-like proteins determine the fate of peptidoglycan during sporulation of Streptomyces coelicolor
    • 16262781
    • Noens EE, Mersinias V, Traag BA, Smith CP, Koerten HK, van Wezel GP (2005) SsgA-like proteins determine the fate of peptidoglycan during sporulation of Streptomyces coelicolor. Mol Microbiol 58:929-944. PMID: 16262781
    • (2005) Mol Microbiol , vol.58 , pp. 929-944
    • Noens, E.E.1    Mersinias, V.2    Traag, B.A.3    Smith, C.P.4    Koerten, H.K.5    Van Wezel, G.P.6
  • 44
    • 0037240661 scopus 로고    scopus 로고
    • A missense mutation in ftsZ differentially affects vegetative and developmentally controlled cell division in Streptomyces coelicolor A3 (2)
    • 12535067
    • Grantcharova N, UbhayasekeraW, Mowbray SL, McCormick JR, Flardh K (2003) A missense mutation in ftsZ differentially affects vegetative and developmentally controlled cell division in Streptomyces coelicolor A3 (2). Mol Microbiol 47:645-656. PMID: 12535067
    • (2003) Mol Microbiol , vol.47 , pp. 645-656
    • Grantcharova, N.1    Ubhayasekera, W.2    Mowbray, S.L.3    McCormick, J.R.4    Flardh, K.5
  • 45
    • 77349099314 scopus 로고    scopus 로고
    • Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way
    • 20487298
    • Molle V, Kremer L (2010) Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way. Mol Microbiol 75:1064-1077. doi: 10.1111/j.1365-2958.2009.07041.x PMID: 20487298
    • (2010) Mol Microbiol , vol.75 , pp. 1064-1077
    • Molle, V.1    Kremer, L.2
  • 46
    • 33845966777 scopus 로고    scopus 로고
    • GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA
    • 17068335
    • Thakur M, Chakraborti PK (2006) GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA. J Biol Chem 281:40107-40113. PMID: 17068335
    • (2006) J Biol Chem , vol.281 , pp. 40107-40113
    • Thakur, M.1    Chakraborti, P.K.2
  • 47
    • 53149116291 scopus 로고    scopus 로고
    • Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis
    • 18557704
    • Thakur M, Chakraborti PK (2008) Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis. Biochem J 415:27-33. doi: 10.1042/BJ20080234 PMID: 18557704
    • (2008) Biochem J , vol.415 , pp. 27-33
    • Thakur, M.1    Chakraborti, P.K.2
  • 48
    • 23044488472 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: Substrate identification and regulation of cell shape
    • 15985609
    • Kang CM, Abbott DW, Park ST, Dascher CC, Cantley LC, Husson RN (2005) The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev 19:1692-1704. PMID: 15985609
    • (2005) Genes Dev , vol.19 , pp. 1692-1704
    • Kang, C.M.1    Abbott, D.W.2    Park, S.T.3    Dascher, C.C.4    Cantley, L.C.5    Husson, R.N.6
  • 49
    • 84879401680 scopus 로고    scopus 로고
    • Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium
    • 23590516
    • Soares NC, Spat P, Krug K, Macek B (2013) Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. J Proteome Res 12:2611-2621. doi: 10.1021/pr3011843 PMID: 23590516
    • (2013) J Proteome Res , vol.12 , pp. 2611-2621
    • Soares, N.C.1    Spat, P.2    Krug, K.3    Macek, B.4
  • 50
    • 84905281353 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC
    • 24390483
    • Ravikumar V, Shi L, Krug K, Derouiche A, Jers C, Cousin C, et al. (2014) Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC. Mol Cell Proteomics 13:1965-1978. doi: 10.1074/mcp. M113.035949 PMID: 24390483
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1965-1978
    • Ravikumar, V.1    Shi, L.2    Krug, K.3    Derouiche, A.4    Jers, C.5    Cousin, C.6
  • 51
    • 82755198873 scopus 로고    scopus 로고
    • Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation
    • 21999169
    • Manteca A, Ye J, Sanchez J, Jensen ON (2011) Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation. J Proteome Res 10:5481-5492. doi: 10.1021/pr200762y PMID: 21999169
    • (2011) J Proteome Res , vol.10 , pp. 5481-5492
    • Manteca, A.1    Ye, J.2    Sanchez, J.3    Jensen, O.N.4
  • 52
    • 77954696406 scopus 로고    scopus 로고
    • Analysis of the phosphoproteome of the multicellular bacterium Streptomyces coelicolor A3 (2) by protein/peptide fractionation, phosphopeptide enrichment and high-accuracy mass spectrometry
    • 20432484
    • Parker JL, Jones AM, Serazetdinova L, Saalbach G, Bibb MJ, Naldrett MJ, (2010) Analysis of the phosphoproteome of the multicellular bacterium Streptomyces coelicolor A3 (2) by protein/peptide fractionation, phosphopeptide enrichment and high-accuracy mass spectrometry. Proteomics 10:2486-2497. doi: 10.1002/pmic.201000090 PMID: 20432484
    • (2010) Proteomics , vol.10 , pp. 2486-2497
    • Parker, J.L.1    Jones, A.M.2    Serazetdinova, L.3    Saalbach, G.4    Bibb, M.J.5    Naldrett, M.J.6
  • 53
    • 84875483830 scopus 로고    scopus 로고
    • Transcriptomic analysis of Streptomyces coelicolor differentiation in solid sporulating cultures: First compartmentalized and second multinucleated mycelia have different and distinctive transcriptomes
    • 23555999
    • Yague P, Rodriguez-Garcia A, Lopez-Garcia MT, Martin JF, Rioseras B, Sanchez J, et al. (2013) Transcriptomic analysis of Streptomyces coelicolor differentiation in solid sporulating cultures: first compartmentalized and second multinucleated mycelia have different and distinctive transcriptomes. PLoS One 8:e60665. doi: 10.1371/journal.pone.0060665 PMID: 23555999
    • (2013) PLoS One , vol.8 , pp. e60665
    • Yague, P.1    Rodriguez-Garcia, A.2    Lopez-Garcia, M.T.3    Martin, J.F.4    Rioseras, B.5    Sanchez, J.6
  • 54
    • 32444446576 scopus 로고    scopus 로고
    • Influence of CrgA on assembly of the cell division protein FtsZ during development of Streptomyces coelicolor
    • 16452438
    • Del Sol R, Mullins JG, Grantcharova N, Flardh K, Dyson P (2006) Influence of CrgA on assembly of the cell division protein FtsZ during development of Streptomyces coelicolor. J Bacteriol 188:1540-1550. PMID: 16452438
    • (2006) J Bacteriol , vol.188 , pp. 1540-1550
    • Del Sol, R.1    Mullins, J.G.2    Grantcharova, N.3    Flardh, K.4    Dyson, P.5
  • 55
    • 33751575802 scopus 로고    scopus 로고
    • Critical residues and novel effects of overexpression of the Streptomyces coelicolor developmental protein BldB: Evidence for a critical interacting partner
    • 16963568
    • Eccleston M, Willems A, Beveridge A, Nodwell JR (2006) Critical residues and novel effects of overexpression of the Streptomyces coelicolor developmental protein BldB: evidence for a critical interacting partner. J Bacteriol 188:8189-8195. PMID: 16963568
    • (2006) J Bacteriol , vol.188 , pp. 8189-8195
    • Eccleston, M.1    Willems, A.2    Beveridge, A.3    Nodwell, J.R.4
  • 56
    • 26944443097 scopus 로고    scopus 로고
    • Identification of a protein Ser/Thr kinase cascade that regulates essential transcriptional activators in Myxococcus xanthus development
    • 16194226
    • Nariya H, Inouye S (2005) Identification of a protein Ser/Thr kinase cascade that regulates essential transcriptional activators in Myxococcus xanthus development. Mol Microbiol 58:367-379. PMID: 16194226
    • (2005) Mol Microbiol , vol.58 , pp. 367-379
    • Nariya, H.1    Inouye, S.2
  • 57
    • 0034731292 scopus 로고    scopus 로고
    • Cloning and characterization of the pknA gene from Streptomyces coelicolor A3(2), coding for the Mn2+ dependent protein Ser/Thr kinase
    • 11162454
    • Petrickova K, Tichy P, Petricek M (2000) Cloning and characterization of the pknA gene from Streptomyces coelicolor A3(2), coding for the Mn2+ dependent protein Ser/Thr kinase. Biochem Biophys Res Commun 279:942-948. PMID: 11162454
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 942-948
    • Petrickova, K.1    Tichy, P.2    Petricek, M.3
  • 60
    • 0031572413 scopus 로고    scopus 로고
    • High efficiency intergeneric conjugal transfer of plasmid DNA from Escherichia coli to methyl DNA-restricting streptomycetes
    • 9351205
    • Flett F, Mersinias V, Smith CP (1997) High efficiency intergeneric conjugal transfer of plasmid DNA from Escherichia coli to methyl DNA-restricting streptomycetes. FEMS Microbiol Lett 155:223-229. PMID: 9351205
    • (1997) FEMS Microbiol Lett , vol.155 , pp. 223-229
    • Flett, F.1    Mersinias, V.2    Smith, C.P.3
  • 61
    • 78049378075 scopus 로고    scopus 로고
    • An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates
    • 20925060
    • Molle V, Leiba J, Zanella-Cleon I, Becchi M, Kremer L (2010) An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates. Proteomics 10:3910-3915. doi: 10.1002/pmic.201000316 PMID: 20925060
    • (2010) Proteomics , vol.10 , pp. 3910-3915
    • Molle, V.1    Leiba, J.2    Zanella-Cleon, I.3    Becchi, M.4    Kremer, L.5
  • 62
    • 77952980794 scopus 로고    scopus 로고
    • Proteogenomics of Pristionchus pacificus reveals distinct proteome structure of nematode models
    • 20237107
    • Borchert N, Dieterich C, Krug K, SchutzW, Jung S, Nordheim A, et al. (2010) Proteogenomics of Pristionchus pacificus reveals distinct proteome structure of nematode models. Genome Res 20:837-846. doi: 10.1101/gr.103119.109 PMID: 20237107
    • (2010) Genome Res , vol.20 , pp. 837-846
    • Borchert, N.1    Dieterich, C.2    Krug, K.3    Schutz, W.4    Jung, S.5    Nordheim, A.6
  • 63
    • 84890487254 scopus 로고    scopus 로고
    • The neuropeptide complement of the marine annelid Platynereis dumerilii
    • 24359412
    • Conzelmann M, Williams EA, Krug K, Franz-Wachtel M, Macek B, Jekely G, (2013) The neuropeptide complement of the marine annelid Platynereis dumerilii. BMC Genomics 14:906. doi: 10.1186/1471-2164-14-906 PMID: 24359412
    • (2013) BMC Genomics , vol.14 , pp. 906
    • Conzelmann, M.1    Williams, E.A.2    Krug, K.3    Franz-Wachtel, M.4    Macek, B.5    Jekely, G.6
  • 64
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p. P. B.-Range mass accuracies and proteome-wide protein quantification
    • 19029910
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p. p. b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26:1367-1372. doi: 10. 1038/nbt.1511 PMID: 19029910
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 65
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: A peptide search engine integrated into the MaxQuant environment
    • 21254760
    • Cox J, Neuhauser N, Michalski A, Scheltema RA, Olsen JV, Mann M. (2011) Andromeda: a peptide search engine integrated into the MaxQuant environment. J Proteome Res 10:1794-1805. doi: 10. 1021/pr101065j PMID: 21254760
    • (2011) J Proteome Res , vol.10 , pp. 1794-1805
    • Cox, J.1    Neuhauser, N.2    Michalski, A.3    Scheltema, R.A.4    Olsen, J.V.5    Mann, M.6
  • 66
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • 9576956
    • Karimova G, Pidoux J, Ullmann A, Ladant D (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci U S A 95:5752-5756. PMID: 9576956
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4


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