메뉴 건너뛰기




Volumn 39, Issue 1, 2011, Pages 259-262

In vitro proof of direct regulation of glutamine synthetase by GlnK proteins in the extreme halophilic archaeon Haloferax mediterranei

Author keywords

Adenylyltransferase (ATase); GlnK; Glutamine synthetase (GS); Haloferax mediterranei; PII

Indexed keywords

BACTERIAL PROTEIN; GLNK PROTEIN; GLUTAMATE AMMONIA LIGASE; UNCLASSIFIED DRUG;

EID: 79551488610     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0390259     Document Type: Conference Paper
Times cited : (10)

References (24)
  • 1
    • 35448984675 scopus 로고    scopus 로고
    • Nitrogen regulation in bacteria and Archaea
    • Leigh, J.A. and Dodsworth, J.A. (2007) Nitrogen regulation in bacteria and Archaea. Annu. Rev. Microbiol. 61, 349-377
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 349-377
    • Leigh, J.A.1    Dodsworth, J.A.2
  • 2
    • 2642530192 scopus 로고    scopus 로고
    • Global carbon/nitrogen control by PII signal transduction in cyanobacteria: From signals to targets
    • Forchhammer, K. (2004) Global carbon/nitrogen control by PII signal transduction in cyanobacteria: from signals to targets. FEMS Microbiol. Rev. 28, 319-333
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 319-333
    • Forchhammer, K.1
  • 4
    • 0035105144 scopus 로고    scopus 로고
    • PII signal transduction proteins, pivotal players in microbial nitrogen control
    • Arcondéguy, T., Jack, R. and Merrick, M. (2001) PII signal transduction proteins, pivotal players in microbial nitrogen control. Microbiol. Mol. Biol. Rev. 65, 80-105
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 80-105
    • Arcondéguy, T.1    Jack, R.2    Merrick, M.3
  • 6
    • 39049106044 scopus 로고    scopus 로고
    • PII signal transducers: Novel functional and structural insights
    • Forchhammer, K. (2008) PII signal transducers: novel functional and structural insights. Trends Microbiol. 16, 65-72
    • (2008) Trends Microbiol. , vol.16 , pp. 65-72
    • Forchhammer, K.1
  • 7
    • 0035976909 scopus 로고    scopus 로고
    • The story of glutamine synthetase regulation
    • Stadtman, E.R. (2001) The story of glutamine synthetase regulation. J. Biol. Chem. 276, 44357-44364
    • (2001) J. Biol. Chem. , vol.276 , pp. 44357-44364
    • Stadtman, E.R.1
  • 8
    • 15944418260 scopus 로고    scopus 로고
    • Unique mechanistic features of post-translational regulation of glutamine synthetase activity in Methanosarcina mazei strain Gö1 in response to nitrogen availability
    • Ehlers, C., Weidenbach, K., Veit, K., Forchhammer, K. and Schmitz, R.A. (2005) Unique mechanistic features of post-translational regulation of glutamine synthetase activity in Methanosarcina mazei strain Gö1 in response to nitrogen availability. Mol. Microbiol. 55, 1841-1854
    • (2005) Mol. Microbiol. , vol.55 , pp. 1841-1854
    • Ehlers, C.1    Weidenbach, K.2    Veit, K.3    Forchhammer, K.4    Schmitz, R.A.5
  • 9
    • 0037083882 scopus 로고    scopus 로고
    • Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB
    • Coutts, G., Thomas, G., Blakey, D. and Merrick, M. (2002) Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB. EMBO J. 21, 536-545
    • (2002) EMBO J. , vol.21 , pp. 536-545
    • Coutts, G.1    Thomas, G.2    Blakey, D.3    Merrick, M.4
  • 10
    • 1542275558 scopus 로고    scopus 로고
    • Ammonium sensing in Escherichia coli: Role of the ammonium transporter AmtB and AmtB-GlnK complex formation
    • Javelle, A., Severi, E., Thornton, J. and Merrick, M. (2004) Ammonium sensing in Escherichia coli: role of the ammonium transporter AmtB and AmtB-GlnK complex formation. J. Biol. Chem. 279, 8530-8538
    • (2004) J. Biol. Chem. , vol.279 , pp. 8530-8538
    • Javelle, A.1    Severi, E.2    Thornton, J.3    Merrick, M.4
  • 11
    • 36549065101 scopus 로고    scopus 로고
    • Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria
    • Huergo, L.F., Merrick, M., Pedrosa, F.O., Chubatsu, L.S., Araujo, L.M. and Souza, E.M. (2007) Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria. Mol. Microbiol. 66, 1523-1535
    • (2007) Mol. Microbiol. , vol.66 , pp. 1523-1535
    • Huergo, L.F.1    Merrick, M.2    Pedrosa, F.O.3    Chubatsu, L.S.4    Araujo, L.M.5    Souza, E.M.6
  • 12
    • 0000549004 scopus 로고
    • Halobacterium mediterranei sp. nov., a new carbohydrate utilizing extreme halophile
    • Rodriguez-Valera, R., Juez, G. and Kushner, D.J. (1983) Halobacterium mediterranei sp. nov., a new carbohydrate utilizing extreme halophile. Syst. Appl. Microbiol. 4, 369-381
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 369-381
    • Rodriguez-Valera, R.1    Juez, G.2    Kushner, D.J.3
  • 15
    • 23744474252 scopus 로고    scopus 로고
    • Development of genetic methods and construction of a chromosomal glnK1 mutant in Methanosarcina mazei strain Gö1
    • Ehlers, C., Weidenbach, K., Veit, K., Deppenmeier, U., Metcalf, W.W. and Schmitz, R.A. (2005) Development of genetic methods and construction of a chromosomal glnK1 mutant in Methanosarcina mazei strain Gö1. Mol. Gen. Genomics 273, 290-298
    • (2005) Mol. Gen. Genomics , vol.273 , pp. 290-298
    • Ehlers, C.1    Weidenbach, K.2    Veit, K.3    Deppenmeier, U.4    Metcalf, W.W.5    Schmitz, R.A.6
  • 17
    • 0033968928 scopus 로고    scopus 로고
    • The glnKamtB operon: A conserved gene pair in prokaryotes
    • Thomas, G., Coutts, G. and Merrick, M. (2000) The glnKamtB operon: a conserved gene pair in prokaryotes. Trends Genet. 16, 11-14
    • (2000) Trends Genet. , vol.16 , pp. 11-14
    • Thomas, G.1    Coutts, G.2    Merrick, M.3
  • 18
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 20
    • 27144454072 scopus 로고    scopus 로고
    • Identification and transcriptional analysis of nitrate assimilation genes in the halophilic archaeon Haloferax mediterranei
    • Lledó, B., Marhuenda-Egea, F.C., Martínez-Espinosa, R.M. and Bonete, M.J. (2005) Identification and transcriptional analysis of nitrate assimilation genes in the halophilic archaeon Haloferax mediterranei. Gene 361, 80-88
    • (2005) Gene , vol.361 , pp. 80-88
    • Lledó, B.1    Marhuenda-Egea, F.C.2    Martínez-Espinosa, R.M.3    Bonete, M.J.4
  • 21
    • 33645978366 scopus 로고    scopus 로고
    • Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei
    • Diaz, S., Perez-Pomares, F., Pire, C., Ferrer, J. and Bonete, M.J. (2006) Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei. Extremophiles 10, 105-115
    • (2006) Extremophiles , vol.10 , pp. 105-115
    • Diaz, S.1    Perez-Pomares, F.2    Pire, C.3    Ferrer, J.4    Bonete, M.J.5
  • 22
    • 0030586251 scopus 로고    scopus 로고
    • NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: Enzyme purification, N-terminal sequence and stability
    • Ferrer, J., Perez-Pomares, F. and Bonete, M.J. (1996) NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: enzyme purification, N-terminal sequence and stability. FEMS Microbiol. Lett. 141, 59-63
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 59-63
    • Ferrer, J.1    Perez-Pomares, F.2    Bonete, M.J.3
  • 23
    • 33749450342 scopus 로고    scopus 로고
    • An octameric prokaryotic glutamine synthetase from the haloarchaeon Haloferax mediterranei
    • Martinez-Espinosa, R.M., Esclapez, J., Bautista, V. and Bonete, M.J. (2006) An octameric prokaryotic glutamine synthetase from the haloarchaeon Haloferax mediterranei. FEMS Microbiol. Lett. 264, 110-116
    • (2006) FEMS Microbiol. Lett. , vol.264 , pp. 110-116
    • Martinez-Espinosa, R.M.1    Esclapez, J.2    Bautista, V.3    Bonete, M.J.4
  • 24
    • 9744219692 scopus 로고    scopus 로고
    • Structure-function studies on the iron-sulfur flavoenzyme glutamate synthase: An unexpectedly complex self-regulated enzyme
    • Vanoni, M.A. and Curti, B. (2005) Structure-function studies on the iron-sulfur flavoenzyme glutamate synthase: an unexpectedly complex self-regulated enzyme. Arch. Biochem. Biophys. 433, 193-211
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 193-211
    • Vanoni, M.A.1    Curti, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.