메뉴 건너뛰기




Volumn 145, Issue 1, 1996, Pages 49-54

Pyrophosphate is a source of phosphoryl groups for Escherichia coli protein phosphorylation

Author keywords

Bacterial protein phosphorylation; Escherichia coli; Phosphate donor; Pyrophosphate

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; BACTERIAL PROTEIN; PYROPHOSPHATE; SERINE;

EID: 0030589112     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1097(96)00384-9     Document Type: Article
Times cited : (6)

References (20)
  • 2
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of rabbit skeletal muscle
    • [2] Krebs, E.G. and Fischer, E.H. (1956) The phosphorylase b to a converting enzyme of rabbit skeletal muscle. Biochim. Biophys. Acta 20, 150-157.
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 150-157
    • Krebs, E.G.1    Fischer, E.H.2
  • 3
    • 0026336662 scopus 로고
    • Protein kinase classification
    • [3] Hunter, T. (1991) Protein kinase classification. Methods Enzymol. 200, 3-37.
    • (1991) Methods Enzymol. , vol.200 , pp. 3-37
    • Hunter, T.1
  • 4
    • 0024149321 scopus 로고
    • Protein phosphorylation in prokaryotes
    • [4] Cozzone, A.J. (1988) Protein phosphorylation in prokaryotes. Annu. Rev. Microbiol. 42, 97-125.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 97-125
    • Cozzone, A.J.1
  • 5
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases: New avenues for cell regulation
    • [5] Shenolikar, S. (1995) Protein serine/threonine phosphatases: new avenues for cell regulation. Annu. Rev. Cell Biol. 10, 55-86.
    • (1995) Annu. Rev. Cell Biol. , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 6
    • 0025006335 scopus 로고
    • Regulation of bacterial physiological processes by three types of protein phosphorylating systems
    • [6] Saier, M.H., Wu, L.F. and Reizer, J. (1990) Regulation of bacterial physiological processes by three types of protein phosphorylating systems. Trends Biochem. Sci. 15, 391-395.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 391-395
    • Saier, M.H.1    Wu, L.F.2    Reizer, J.3
  • 7
    • 0028138668 scopus 로고
    • Histidine and aspartate phosphorylation: Two-component systems and the limits of homology
    • [7] Swanson, R.V., Alex, L.A. and Simon, M.I. (1994) Histidine and aspartate phosphorylation: two-component systems and the limits of homology. Trends Biochem. Sci. 19, 485-490.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 485-490
    • Swanson, R.V.1    Alex, L.A.2    Simon, M.I.3
  • 8
    • 0028245628 scopus 로고
    • Light signals are transduced to the phosphorylation of 15 kDa proteins in Neurospora crassa
    • [8] Oda, K. and Hasunuma, K. (1994) Light signals are transduced to the phosphorylation of 15 kDa proteins in Neurospora crassa. FEBS Lett. 345, 162-166.
    • (1994) FEBS Lett. , vol.345 , pp. 162-166
    • Oda, K.1    Hasunuma, K.2
  • 9
    • 0027380220 scopus 로고
    • Arabidopsis ethylene response gene ETR 1: Similarity of product to two-component regulators
    • [9] Chang, C., Kwok, S.F., Bleecker, A.B. and Meyerowitz, E.M. (1993) Arabidopsis ethylene response gene ETR 1: similarity of product to two-component regulators. Science 262, 539-544.
    • (1993) Science , vol.262 , pp. 539-544
    • Chang, C.1    Kwok, S.F.2    Bleecker, A.B.3    Meyerowitz, E.M.4
  • 10
    • 0027507956 scopus 로고
    • A yeast protein similar to bacterial two-component regulators
    • [10] Ota, I.M. and Varshavsky, A. (1993) A yeast protein similar to bacterial two-component regulators. Science 262, 566-569.
    • (1993) Science , vol.262 , pp. 566-569
    • Ota, I.M.1    Varshavsky, A.2
  • 11
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate : Carbohydrate phosphotransferase systems of bacteria
    • [11] Postma, P.W., Lengeler, J.W. and Jacobson, G.R. (1993) Phosphoenolpyruvate : carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57, 543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 12
    • 0027207516 scopus 로고
    • Is acetylphosphate a global signal in Escherichia coli?
    • [12] McCleary, W.R., Stock, J.B. and Ninfa, A.J. (1993) Is acetylphosphate a global signal in Escherichia coli? J. Bacteriol. 175, 2793-2798.
    • (1993) J. Bacteriol. , vol.175 , pp. 2793-2798
    • McCleary, W.R.1    Stock, J.B.2    Ninfa, A.J.3
  • 13
    • 0020393472 scopus 로고
    • Endogenous protein phosphorylation in Escherichia coli extracts
    • [13] Manai, M. and Cozzone, A.J. (1982) Endogenous protein phosphorylation in Escherichia coli extracts. Biochem. Biophys. Res. Commun. 107, 981-988.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 981-988
    • Manai, M.1    Cozzone, A.J.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • [14] Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • [15] Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • [16] Duclos, B., Marcandier, S. and Cozzone, A.J. (1991) Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis. Methods Enzymol. 201, 10-21.
    • (1991) Methods Enzymol. , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A.J.3
  • 17
    • 0028868237 scopus 로고
    • Overproduction, purification and structural characterization of the functional N-terminal DNA-binding domain of the fru represser from Escherichia coli K-12
    • [17] Scarabel, M., Penin, F., Bonod, C., Nègre, D., Cozzone, A.J. and Cortay, J.C. (1995) Overproduction, purification and structural characterization of the functional N-terminal DNA-binding domain of the fru represser from Escherichia coli K-12. Gene 153, 9-15.
    • (1995) Gene , vol.153 , pp. 9-15
    • Scarabel, M.1    Penin, F.2    Bonod, C.3    Nègre, D.4    Cozzone, A.J.5    Cortay, J.C.6
  • 18
    • 0030010395 scopus 로고    scopus 로고
    • Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues
    • [18] Rittinger, K., Nègre, D., Divita, G., Scarabel, M., Bonod, C., Goody, R.S., Cozzone, A.J. and Cortay, J.C. (1996) Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues. Eur. J. Biochem. 237, 247-254.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 247-254
    • Rittinger, K.1    Nègre, D.2    Divita, G.3    Scarabel, M.4    Bonod, C.5    Goody, R.S.6    Cozzone, A.J.7    Cortay, J.C.8
  • 19
    • 0002318614 scopus 로고
    • Expression and purification of glutathione s-transferase fusion proteins
    • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (Eds.)
    • [19] Smith, D.B. and Corcoran, L.M. (1990) Expression and purification of glutathione S-transferase fusion proteins. In : Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (Eds.), Current Protocols in Molecular Biology.
    • (1990) Current Protocols in Molecular Biology
    • Smith, D.B.1    Corcoran, L.M.2
  • 20
    • 0025277420 scopus 로고
    • Occurrence of protein phosphorylation in various bacterial species
    • [20] Dadssi, M. and Cozzone, A.J. (1990) Occurrence of protein phosphorylation in various bacterial species. Int. J. Biochem. 22, 493-499.
    • (1990) Int. J. Biochem. , vol.22 , pp. 493-499
    • Dadssi, M.1    Cozzone, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.