메뉴 건너뛰기




Volumn 275, Issue 24, 2008, Pages 6237-6247

Identification, characterization and activation mechanism of a tyrosine kinase of Bacillus anthracis

Author keywords

Bacillus anthracis; ITC; McsB; SPR; Tyrosine kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE MCSA; PROTEIN TYROSINE KINASE MCSB; UNCLASSIFIED DRUG;

EID: 56849102152     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06748.x     Document Type: Article
Times cited : (3)

References (41)
  • 1
    • 0032728879 scopus 로고    scopus 로고
    • Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB
    • Gay YA, Jamil S Drews SJ (1999) Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB. Infect Immun 67, 5676 5682.
    • (1999) Infect Immun , vol.67 , pp. 5676-5682
    • Gay, Y.A.1    Jamil, S.2    Drews, S.J.3
  • 2
    • 0036428610 scopus 로고    scopus 로고
    • Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis implicated in developmental processes
    • Madec E, Laszkiewicz A, Iwanicki A, Obuchowski M Simone S (2002) Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis implicated in developmental processes. Mol Microbiol 2, 571 586.
    • (2002) Mol Microbiol , vol.2 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Simone, S.5
  • 4
    • 33846683630 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: An emerging regulatory device of bacterial physiology
    • Grangeasse C, Cozzone AJ, Deutscher J Mijakovic I (2006) Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem Sci 32, 86 94.
    • (2006) Trends Biochem Sci , vol.32 , pp. 86-94
    • Grangeasse, C.1    Cozzone, A.J.2    Deutscher, J.3    Mijakovic, I.4
  • 5
    • 27144440950 scopus 로고    scopus 로고
    • A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis
    • Kirstein J, Zühlke D, Gerth U, Turgay K Hecker M (2005) A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis. EMBO J 24, 3435 3445.
    • (2005) EMBO J , vol.24 , pp. 3435-3445
    • Kirstein, J.1    Zühlke, D.2    Gerth, U.3    Turgay, K.4    Hecker, M.5
  • 6
    • 30744478198 scopus 로고    scopus 로고
    • Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens
    • Cozzone AJ (2005) Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens. J Mol Microbiol Biotechnol 9, 198 213.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 198-213
    • Cozzone, A.J.1
  • 7
    • 0037384743 scopus 로고    scopus 로고
    • Phosphorylation-mediated regulation of heat shock response in Escherichia coli
    • Klein G, Dartigalongue C Raina S (2003) Phosphorylation-mediated regulation of heat shock response in Escherichia coli. Mol Microbiol 48, 269 285.
    • (2003) Mol Microbiol , vol.48 , pp. 269-285
    • Klein, G.1    Dartigalongue, C.2    Raina, S.3
  • 8
    • 0141574316 scopus 로고    scopus 로고
    • Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase
    • Grangeasse C, Obadia B, Mijakovic I, Deutscher J, Cozzone AJ Double P (2003) Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. J Biol Chem 278, 39323 39329.
    • (2003) J Biol Chem , vol.278 , pp. 39323-39329
    • Grangeasse, C.1    Obadia, B.2    Mijakovic, I.3    Deutscher, J.4    Cozzone, A.J.5    Double, P.6
  • 12
    • 33749597441 scopus 로고    scopus 로고
    • Comparative analysis of two-component signal transduction systems of Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis
    • de Been M, Francke C, Moezelaar R, Abee T Siezen RJ (2006) Comparative analysis of two-component signal transduction systems of Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis. Microbiology 152, 3035 3048.
    • (2006) Microbiology , vol.152 , pp. 3035-3048
    • De Been, M.1    Francke, C.2    Moezelaar, R.3    Abee, T.4    Siezen, R.J.5
  • 14
    • 2342659731 scopus 로고    scopus 로고
    • Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC, which encodes the repressor for the alkaline exoprotease gene, aprE
    • 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
  • 16
    • 0034120118 scopus 로고    scopus 로고
    • Control of sporulation gene expression in Bacillus subtlis by the chromosome partitioning protein Soj (ParA) and Spo0J (ParB)
    • Quisel JD Grossman AD (2000) Control of sporulation gene expression in Bacillus subtlis by the chromosome partitioning protein Soj (ParA) and Spo0J (ParB). J Bacteriol 182, 3446 3451.
    • (2000) J Bacteriol , vol.182 , pp. 3446-3451
    • Quisel, J.D.1    Grossman, A.D.2
  • 17
    • 0031765193 scopus 로고    scopus 로고
    • Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis
    • Levin PA, Shim JJ Grossman AD (1998) Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis. J Bacteriol 180, 6048 6051.
    • (1998) J Bacteriol , vol.180 , pp. 6048-6051
    • Levin, P.A.1    Shim, J.J.2    Grossman, A.D.3
  • 18
    • 27644472372 scopus 로고    scopus 로고
    • Orthologs, paralogs, and evolutionary genomics
    • Koonin EV (2005) Orthologs, paralogs, and evolutionary genomics. Annu Rev Genet 39, 309 338.
    • (2005) Annu Rev Genet , vol.39 , pp. 309-338
    • Koonin, E.V.1
  • 21
    • 3042856467 scopus 로고    scopus 로고
    • The active site cysteine of arginine kinase, structural and functional analysis of partially active mutants
    • Gattis JL, Ruben E, Fenley MO, Ellington WR Chapman MS (2004) The active site cysteine of arginine kinase, structural and functional analysis of partially active mutants. Biochemistry 43, 8680 8689.
    • (2004) Biochemistry , vol.43 , pp. 8680-8689
    • Gattis, J.L.1    Ruben, E.2    Fenley, M.O.3    Ellington, W.R.4    Chapman, M.S.5
  • 22
    • 33744913312 scopus 로고    scopus 로고
    • Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism
    • Soulat D, Jault JM, Duclos B, Geourjon C, Cozzone AJ Grangeasse C (2006) Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism. J Biol Chem 281, 14048 14056.
    • (2006) J Biol Chem , vol.281 , pp. 14048-14056
    • Soulat, D.1    Jault, J.M.2    Duclos, B.3    Geourjon, C.4    Cozzone, A.J.5    Grangeasse, C.6
  • 25
    • 33751539464 scopus 로고    scopus 로고
    • Protein-protein interactions in the allosteric regulation of protein kinases
    • Pellicena P Kuriyan J (2006) Protein-protein interactions in the allosteric regulation of protein kinases. Curr Opin Struct Biol 16, 702 709.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 702-709
    • Pellicena, P.1    Kuriyan, J.2
  • 27
    • 0032705126 scopus 로고    scopus 로고
    • Nucleotide binding to creatine kinase: An isothermal titration microcalorimetry study
    • Forstner M, Berger C Wallimann T (1999) Nucleotide binding to creatine kinase: an isothermal titration microcalorimetry study. FEBS Lett 461, 111 114.
    • (1999) FEBS Lett , vol.461 , pp. 111-114
    • Forstner, M.1    Berger, C.2    Wallimann, T.3
  • 28
    • 12144285772 scopus 로고    scopus 로고
    • Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: Binding, kinetic, and crystallographic studies with ATP and MgATP
    • Flachner B, Kovari Z, Varga A, Gugolya Z, Vonderviszt F, Szabo GN Vas M (2004) Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. Biochemistry 43, 3436 3449.
    • (2004) Biochemistry , vol.43 , pp. 3436-3449
    • Flachner, B.1    Kovari, Z.2    Varga, A.3    Gugolya, Z.4    Vonderviszt, F.5    Szabo, G.N.6    Vas, M.7
  • 29
    • 13544250497 scopus 로고    scopus 로고
    • Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes
    • Abraham T, Lewis RN, Hodges RS McElhaney RN (2005) Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes. Biochemistry 44, 2103 2112.
    • (2005) Biochemistry , vol.44 , pp. 2103-2112
    • Abraham, T.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 30
    • 33746824856 scopus 로고
    • Hydrophobic effects - Opinion and facts
    • Blokzijl W Engberts JBFN (1993) Hydrophobic effects - opinion and facts. Angew Chem Intl Ed Engl 32, 1545 1579.
    • (1993) Angew Chem Intl Ed Engl , vol.32 , pp. 1545-1579
    • Blokzijl, W.1    Jbfn, E.2
  • 31
    • 30544441077 scopus 로고    scopus 로고
    • Water's hydrogen bond in the hydrophobic effect: A simple model
    • Xu H Dill KA (2005) Water's hydrogen bond in the hydrophobic effect: a simple model. J Phys Chem B 109, 23611 23617.
    • (2005) J Phys Chem B , vol.109 , pp. 23611-23617
    • Xu, H.1    Dill, K.A.2
  • 32
    • 0008023849 scopus 로고    scopus 로고
    • Hydrophobic effect, water structure, and heat capacity changes
    • Sharp KA Madan B (1997) Hydrophobic effect, water structure, and heat capacity changes. J Phys Chem B 101, 4343 4348.
    • (1997) J Phys Chem B , vol.101 , pp. 4343-4348
    • Sharp, K.A.1    Madan, B.2
  • 33
    • 0029042647 scopus 로고
    • Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase
    • Kresheck GC, Vitello LB Erman JE (1995) Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase. Biochemistry 34, 8398 8405.
    • (1995) Biochemistry , vol.34 , pp. 8398-8405
    • Kresheck, G.C.1    Vitello, L.B.2    Erman, J.E.3
  • 34
    • 0027942020 scopus 로고
    • + reductase and the role of water at the complex interface
    • + reductase and the role of water at the complex interface. Biochemistry 33, 13321 13328.
    • (1994) Biochemistry , vol.33 , pp. 13321-13328
    • Jelesarov, I.1    Bosshard, H.R.2
  • 35
    • 3342931068 scopus 로고    scopus 로고
    • A mechanism-based cross-linker for the identification of kinase-substrate pairs
    • Maly DJ, Allen JA Shokat KM (2004) A mechanism-based cross-linker for the identification of kinase-substrate pairs. J Am Chem Soc 126, 9160 9161.
    • (2004) J Am Chem Soc , vol.126 , pp. 9160-9161
    • Maly, D.J.1    Allen, J.A.2    Shokat, K.M.3
  • 36
    • 18744429842 scopus 로고    scopus 로고
    • Hitting the target: Emerging technologies in the search for kinase substrates
    • Manning BD Cantley LC (2002) Hitting the target: emerging technologies in the search for kinase substrates. Sci STKE 162, 1 4.
    • (2002) Sci STKE , vol.162 , pp. 1-4
    • Manning, B.D.1    Cantley, L.C.2
  • 37
  • 39
    • 0037321548 scopus 로고    scopus 로고
    • Kinetic analysis of estrogen receptor homo- and heterodimerization in vitro
    • Jisa E Jungbauer A (2003) Kinetic analysis of estrogen receptor homo- and heterodimerization in vitro. J Steroid Biochem Mol Biol 84, 141 148.
    • (2003) J Steroid Biochem Mol Biol , vol.84 , pp. 141-148
    • Jisa, E.1    Jungbauer, A.2
  • 40
    • 0032519984 scopus 로고    scopus 로고
    • Nucleotide-binding properties of kinase deficient epidermal-growth-factor receptor mutants
    • Kunrong C Koland JG (1998) Nucleotide-binding properties of kinase deficient epidermal-growth-factor receptor mutants. Biochem J 330, 353 359.
    • (1998) Biochem J , vol.330 , pp. 353-359
    • Kunrong, C.1    Koland, J.G.2
  • 41
    • 0347356332 scopus 로고    scopus 로고
    • Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: Evidence for interaction between ATP and Trp653
    • Ramaen O, Masscheleyn S, Duffieux F, Pamlard O, Oberkampf M, Lallemand JY, Stoven V Jacquet E (2003) Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653. Biochem J 376, 749 756.
    • (2003) Biochem J , vol.376 , pp. 749-756
    • Ramaen, O.1    Masscheleyn, S.2    Duffieux, F.3    Pamlard, O.4    Oberkampf, M.5    Lallemand, J.Y.6    Stoven, V.7    Jacquet, E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.