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Volumn 62, Issue 1, 2016, Pages 67-70

Evolution and tinkering: what do a protein kinase, a transcriptional regulator and chromosome segregation/cell division proteins have in common?

Author keywords

ATPase; Cell division; Divergent evolution; DNA binding domain; Protein phosphorylation; Transcriptional regulation

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; CHROMOSOME PROTEIN; MIND PROTEIN; PROTEIN KINASE; PROTEIN TYROSINE KINASE; PTKA PROTEIN; SALA PROTEIN; SOJ PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; PROTEIN BINDING;

EID: 84955731135     PISSN: 01728083     EISSN: 14320983     Source Type: Journal    
DOI: 10.1007/s00294-015-0513-y     Document Type: Review
Times cited : (11)

References (25)
  • 1
    • 0037221304 scopus 로고    scopus 로고
    • A role for division-site-selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis
    • COI: 1:CAS:528:DC%2BD3sXntVKhsQ%3D%3D, PID: 1249286
    • Autret S, Errington J (2003) A role for division-site-selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis. Mol Microbiol 47:159–169
    • (2003) Mol Microbiol , vol.47 , pp. 159-169
    • Autret, S.1    Errington, J.2
  • 2
    • 0025780692 scopus 로고
    • Locations of the metG and mrp genes on the physical map of Escherichia coli
    • COI: 1:CAS:528:DyaK3MXkt1egt7Y%3D, PID: 167520
    • Dardel F, Panvert M, Blanquet S, Fayat G (1991) Locations of the metG and mrp genes on the physical map of Escherichia coli. J Bacteriol 173:3273
    • (1991) J Bacteriol , vol.173 , pp. 3273
    • Dardel, F.1    Panvert, M.2    Blanquet, S.3    Fayat, G.4
  • 3
    • 84890089222 scopus 로고    scopus 로고
    • Interaction of bacterial fatty-acid-displaced regulators with DNA is interrupted by tyrosine phosphorylation in the helix–turn–helix domain
    • COI: 1:CAS:528:DC%2BC3sXhslWrt7fE, PID: 2393961
    • Derouiche A, Bidnenko V, Grenha R, Pigonneau N, Ventroux M, Franz-Wachtel M, Nessler S, Noirot-Gros MF, Mijakovic I (2013) Interaction of bacterial fatty-acid-displaced regulators with DNA is interrupted by tyrosine phosphorylation in the helix–turn–helix domain. Nucleic Acids Res 41:9371–9381
    • (2013) Nucleic Acids Res , vol.41 , pp. 9371-9381
    • Derouiche, A.1    Bidnenko, V.2    Grenha, R.3    Pigonneau, N.4    Ventroux, M.5    Franz-Wachtel, M.6    Nessler, S.7    Noirot-Gros, M.F.8    Mijakovic, I.9
  • 5
    • 38849192336 scopus 로고    scopus 로고
    • Modeling protein network evolution under genome duplication and domain shuffling
    • PID: 1799976
    • Evlampiev K, Isamberth H (2007) Modeling protein network evolution under genome duplication and domain shuffling. BMC Syst Biol 1:49
    • (2007) BMC Syst Biol , vol.1 , pp. 49
    • Evlampiev, K.1    Isamberth, H.2
  • 6
    • 84865095336 scopus 로고    scopus 로고
    • Bacterial tyrosine kinases: evolution, biological function and structural insights
    • COI: 1:CAS:528:DC%2BC38XhtlGrur%2FL, PID: 2288991
    • Grangeasse C, Nessler S, Mijakovic I (2012) Bacterial tyrosine kinases: evolution, biological function and structural insights. Philos Trans R Soc Lond B Biol Sci 367:2640–2655
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 2640-2655
    • Grangeasse, C.1    Nessler, S.2    Mijakovic, I.3
  • 7
    • 0030989408 scopus 로고    scopus 로고
    • Three-dimensional domain duplication, swapping and stealing
    • COI: 1:CAS:528:DyaK2sXjvFWjsr0%3D, PID: 920428
    • Heringa J, Taylor WR (1997) Three-dimensional domain duplication, swapping and stealing. Curr Opin Struct Biol 7:416–421
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 416-421
    • Heringa, J.1    Taylor, W.R.2
  • 8
    • 0017771466 scopus 로고
    • Evolution and tinkering
    • COI: 1:STN:280:DyaE2s7nsVKqug%3D%3D, PID: 86013
    • Jacob F (1977) Evolution and tinkering. Science 196:1161–1166
    • (1977) Science , vol.196 , pp. 1161-1166
    • Jacob, F.1
  • 10
    • 84865105858 scopus 로고    scopus 로고
    • Evolution of SH2 domains and phosphotyrosine signalling networks
    • COI: 1:CAS:528:DC%2BC38XhtlGrur7K, PID: 2288990
    • Liu BA, Nash PD (2012) Evolution of SH2 domains and phosphotyrosine signalling networks. Philos Trans R Soc Lond B Biol Sci 367:2556–2573
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 2556-2573
    • Liu, B.A.1    Nash, P.D.2
  • 11
    • 0032973292 scopus 로고    scopus 로고
    • Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC
    • COI: 1:CAS:528:DyaK1MXksFGrsL0%3D, PID: 1041172
    • Marston AL, Errington J (1999) Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC. Mol Microbiol 33:84–96
    • (1999) Mol Microbiol , vol.33 , pp. 84-96
    • Marston, A.L.1    Errington, J.2
  • 14
    • 52949106530 scopus 로고    scopus 로고
    • Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA
    • COI: 1:CAS:528:DC%2BD1cXht1Gkt7nI, PID: 1885415
    • Murray H, Errington J (2008) Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA. Cell 135:74–84
    • (2008) Cell , vol.135 , pp. 74-84
    • Murray, H.1    Errington, J.2
  • 15
    • 2342659731 scopus 로고    scopus 로고
    • Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC, which encodes the repressor for the alkaline exoprotease gene, aprE
    • COI: 1:CAS:528:DC%2BD2cXktVGhurg%3D, PID: 1512646
    • Ogura M, Matsuzawa A, Yoshikawa H, Tanaka T (2004) Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC, which encodes the repressor for the alkaline exoprotease gene, aprE. J Bacteriol 186:3056–3064
    • (2004) J Bacteriol , vol.186 , pp. 3056-3064
    • Ogura, M.1    Matsuzawa, A.2    Yoshikawa, H.3    Tanaka, T.4
  • 18
    • 33947263138 scopus 로고    scopus 로고
    • Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication
    • COI: 1:CAS:528:DC%2BD2sXksVWltr4%3D, PID: 1736739
    • Petranovic D, Michelsen O, Zahradka K, Silva C, Petranovic M, Jensen PR, Mijakovic I (2007) Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication. Mol Microbiol 63:1797–1805
    • (2007) Mol Microbiol , vol.63 , pp. 1797-1805
    • Petranovic, D.1    Michelsen, O.2    Zahradka, K.3    Silva, C.4    Petranovic, M.5    Jensen, P.R.6    Mijakovic, I.7
  • 19
    • 79551683984 scopus 로고    scopus 로고
    • Spo0 J regulates the oligomeric state of Soj to trigger its switch from an activator to an inhibitor of DNA replication initiation
    • COI: 1:CAS:528:DC%2BC3MXjt1amu7o%3D, PID: 2123564
    • Scholefield G, Whiting R, Errington J, Murray H (2011) Spo0 J regulates the oligomeric state of Soj to trigger its switch from an activator to an inhibitor of DNA replication initiation. Mol Microbiol 79:1089–1100
    • (2011) Mol Microbiol , vol.79 , pp. 1089-1100
    • Scholefield, G.1    Whiting, R.2    Errington, J.3    Murray, H.4
  • 20
    • 84858794276 scopus 로고    scopus 로고
    • Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA
    • COI: 1:CAS:528:DC%2BC38Xht1ejsLk%3D, PID: 2228694
    • Scholefield G, Errington J, Murray H (2012) Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA. EMBO J 31:1542–1555
    • (2012) EMBO J , vol.31 , pp. 1542-1555
    • Scholefield, G.1    Errington, J.2    Murray, H.3
  • 21
    • 84987819734 scopus 로고    scopus 로고
    • Protein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talk
    • PID: 2537456
    • Shi L, Pigeonneau N, Ventroux M, Derouiche A, Bidnenko V, Mijakovic I, Noirot-Gros MF (2014) Protein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talk. Front Microbiol 5:538
    • (2014) Front Microbiol , vol.5 , pp. 538
    • Shi, L.1    Pigeonneau, N.2    Ventroux, M.3    Derouiche, A.4    Bidnenko, V.5    Mijakovic, I.6    Noirot-Gros, M.F.7
  • 23
    • 33847634233 scopus 로고    scopus 로고
    • Evidence of interaction network evolution by whole-genome duplications: a case study in MADS-box proteins
    • COI: 1:CAS:528:DC%2BD2sXjtlersro%3D, PID: 1717552
    • Veron AS, Kaufmann K, Bornberg-Bauer E (2007) Evidence of interaction network evolution by whole-genome duplications: a case study in MADS-box proteins. Mol Biol Evol 24:670–680
    • (2007) Mol Biol Evol , vol.24 , pp. 670-680
    • Veron, A.S.1    Kaufmann, K.2    Bornberg-Bauer, E.3
  • 24
    • 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
    • COI: 1:CAS:528:DyaL3sXhtVensbY%3D, PID: 632971
    • 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
  • 25
    • 79952450528 scopus 로고    scopus 로고
    • Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC
    • COI: 1:CAS:528:DC%2BC3MXkslSktb8%3D, PID: 2123196
    • Wu W, Park KT, Holyoak T, Lutkenhaus J (2011) Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol Microbiol 79:1515–1528
    • (2011) Mol Microbiol , vol.79 , pp. 1515-1528
    • Wu, W.1    Park, K.T.2    Holyoak, T.3    Lutkenhaus, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.