메뉴 건너뛰기




Volumn 1834, Issue 1, 2013, Pages 16-23

Regulation of ammonium assimilation in Haloferax mediterranei: Interaction between glutamine synthetase and two GlnK proteins

Author keywords

2 oxoglutarate; GlnK; Glutamine synthetase; Haloferax mediterranei; Nitrogen metabolism regulation; PII

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; GLNK 1 PROTEIN; GLNK 2 PROTEIN; GLUTAMATE AMMONIA LIGASE; PROTEIN; UNCLASSIFIED DRUG;

EID: 84869878582     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.10.006     Document Type: Article
Times cited : (21)

References (26)
  • 1
    • 35448984675 scopus 로고    scopus 로고
    • Nitrogen regulation in bacteria and archaea
    • J.A. Leigh, and J.A. Dodsworth Nitrogen regulation in bacteria and archaea Annu. Rev. Microbiol. 61 2007 349 377
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 349-377
    • Leigh, J.A.1    Dodsworth, J.A.2
  • 2
    • 0035105144 scopus 로고    scopus 로고
    • PII signal transduction proteins, pivotal players in microbial nitrogen control
    • T. Arcondéguy, R. Jack, and M. Merrick PII signal transduction proteins, pivotal players in microbial nitrogen control Microbiol. Mol. Biol. Rev. 65 2001 80 105
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 80-105
    • Arcondéguy, T.1    Jack, R.2    Merrick, M.3
  • 3
    • 2642530192 scopus 로고    scopus 로고
    • Global carbon/nitrogen control by PII signal transduction in cyanobacteria: From signals to targets
    • K. Forchhammer Global carbon/nitrogen control by PII signal transduction in cyanobacteria: from signals to targets FEMS Microbiol. Rev. 28 2004 319 333
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 319-333
    • Forchhammer, K.1
  • 4
    • 39049106044 scopus 로고    scopus 로고
    • PII signal transducers: Novel functional and structural insights
    • K. Forchhammer PII signal transducers: novel functional and structural insights Trends Microbiol. 16 2008 65 72
    • (2008) Trends Microbiol. , vol.16 , pp. 65-72
    • Forchhammer, K.1
  • 5
    • 84873303080 scopus 로고    scopus 로고
    • PII signal transduction proteins: Nitrogen regulation and beyond
    • 10.1111/j.1574-6976.2012.00351
    • L.F. Huergo, G. Chandra, and M. Merrick PII signal transduction proteins: nitrogen regulation and beyond FEMS Microbiol. Rev. July 26 2012 10.1111/j.1574-6976.2012.00351
    • (2012) FEMS Microbiol. Rev.
    • Huergo, L.F.1    Chandra, G.2    Merrick, M.3
  • 6
    • 34047208419 scopus 로고    scopus 로고
    • Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): Kinetic characterization of regulation by PII, PII-UMP, glutamine, and α-ketoglutarate
    • P. Jiang, A.E. Mayo, and A.J. Ninfa Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and α-ketoglutarate Biochemistry 46 2007 4133 4146
    • (2007) Biochemistry , vol.46 , pp. 4133-4146
    • Jiang, P.1    Mayo, A.E.2    Ninfa, A.J.3
  • 7
    • 1542275558 scopus 로고    scopus 로고
    • Ammonium sensing in Escherichia coli. Role of the ammonium transporter AmtB and AmtB-GlnK complex formation
    • A. Javelle, E. Severi, J. Thornton, and M. Merrick Ammonium sensing in Escherichia coli. Role of the ammonium transporter AmtB and AmtB-GlnK complex formation J. Biol. Chem. 279 2004 8530 8538
    • (2004) J. Biol. Chem. , vol.279 , pp. 8530-8538
    • Javelle, A.1    Severi, E.2    Thornton, J.3    Merrick, M.4
  • 8
    • 2942628873 scopus 로고    scopus 로고
    • The Synechococcus elongates PII signal transduction protein controls arginine synthesis by complex formation with N-acetyl-l-glutamate kinase
    • A. Heinrich, M. Maheswaran, U. Ruppert, and K. Forchhammer The Synechococcus elongates PII signal transduction protein controls arginine synthesis by complex formation with N-acetyl-l-glutamate kinase Mol. Microbiol. 52 2004 1303 1314
    • (2004) Mol. Microbiol. , vol.52 , pp. 1303-1314
    • Heinrich, A.1    Maheswaran, M.2    Ruppert, U.3    Forchhammer, K.4
  • 9
    • 4344704870 scopus 로고    scopus 로고
    • Genetic regulation of biological nitrogen fixation
    • R. Dixon, and D. Kahn Genetic regulation of biological nitrogen fixation Nat. Rev. Microbiol. 621 2004 621 631
    • (2004) Nat. Rev. Microbiol. , vol.621 , pp. 621-631
    • Dixon, R.1    Kahn, D.2
  • 10
    • 76249096491 scopus 로고    scopus 로고
    • Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate - Regulated by interaction of PII with the biotin carboxyl carrier subunit
    • A.B. Feria Bourrellier, B. Valot, A. Guillot, F. Ambard-Bretteville, J. Vidal, and M. Hodges Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate - regulated by interaction of PII with the biotin carboxyl carrier subunit Proc. Natl. Acad. Sci. U. S. A. 107 2010 502 507
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 502-507
    • Feria Bourrellier, A.B.1    Valot, B.2    Guillot, A.3    Ambard-Bretteville, F.4    Vidal, J.5    Hodges, M.6
  • 11
    • 33845942520 scopus 로고    scopus 로고
    • Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis
    • A. Heinrich, K. Woyda, K. Brauburger, G. Meiss, C. Detsch, J. Stülke, and K. Forchhammer Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis J. Biol. Chem. 281 2006 34909 34917
    • (2006) J. Biol. Chem. , vol.281 , pp. 34909-34917
    • Heinrich, A.1    Woyda, K.2    Brauburger, K.3    Meiss, G.4    Detsch, C.5    Stülke, J.6    Forchhammer, K.7
  • 12
    • 0036007437 scopus 로고    scopus 로고
    • Characterization of GlnK1 from Methanosarcina mazei Strain Gö1: Complementation of an Escherichia coli glnK Mutant Strain by GlnK1
    • C. Ehlers, R. Grabbe, K. Veit, and R.A. Schmitz Characterization of GlnK1 from Methanosarcina mazei Strain Gö1: complementation of an Escherichia coli glnK Mutant Strain by GlnK1 J. Bacteriol. 184 2002 1028 1040
    • (2002) J. Bacteriol. , vol.184 , pp. 1028-1040
    • Ehlers, C.1    Grabbe, R.2    Veit, K.3    Schmitz, R.A.4
  • 13
    • 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
    • C. Ehlers, K. Weidenbach, K. Veit, K. Forchhammer, and R.A. Schmitz Unique mechanistic features of post-translational regulation of glutamine synthetase activity in Methanosarcina mazei strain Gö1 in response to nitrogen availability Mol. Microbiol. 55 2005 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
  • 14
    • 77956176486 scopus 로고    scopus 로고
    • Cooperative binding of MgATP and MgADP in the trimeric PII protein GlnK2 from Archaeoglobus fulgidus
    • S. Helfmann, W. Lü, C. Litz, and S.L.A. Andrade Cooperative binding of MgATP and MgADP in the trimeric PII protein GlnK2 from Archaeoglobus fulgidus J. Mol. Biol. 402 2010 165 177
    • (2010) J. Mol. Biol. , vol.402 , pp. 165-177
    • Helfmann, S.1    Lü, W.2    Litz, C.3    Andrade, S.L.A.4
  • 15
    • 79951471045 scopus 로고    scopus 로고
    • Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus
    • C. Litz, S. Helfmann, S. Gerhardt, and S.L.A. Andrade Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus Acta Crystallogr. 67 2011 178 181
    • (2011) Acta Crystallogr. , vol.67 , pp. 178-181
    • Litz, C.1    Helfmann, S.2    Gerhardt, S.3    Andrade, S.L.A.4
  • 16
    • 0000549004 scopus 로고
    • Halobacterium mediterranei sp. nov., a new carbohydrate utilizing extreme halophile
    • R. Rodriguez-Valera, G. Juez, and D.J. Kushner Halobacterium mediterranei sp. nov., a new carbohydrate utilizing extreme halophile Syst. Appl. Microbiol. 4 1983 369 381
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 369-381
    • Rodriguez-Valera, R.1    Juez, G.2    Kushner, D.J.3
  • 18
    • 79551488610 scopus 로고    scopus 로고
    • In vitro proof of direct regulation of glutamine synthetase by GlnK proteins in the extreme halophilic archaeon Haloferax mediterranei
    • L. Pedro-Roig, M. Camacho, and M.J. Bonete In vitro proof of direct regulation of glutamine synthetase by GlnK proteins in the extreme halophilic archaeon Haloferax mediterranei Biochem. Soc. Trans. 39 2011 259 262
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 259-262
    • Pedro-Roig, L.1    Camacho, M.2    Bonete, M.J.3
  • 19
    • 0014903044 scopus 로고
    • The regulation of glutamine synthetase in microorganisms
    • B.M. Shapiro, and E.R. Stadtman The regulation of glutamine synthetase in microorganisms Annu. Rev. Microbiol. 24 1970 501 524
    • (1970) Annu. Rev. Microbiol. , vol.24 , pp. 501-524
    • Shapiro, B.M.1    Stadtman, E.R.2
  • 20
    • 33749450342 scopus 로고    scopus 로고
    • An octameric prokaryotic glutamine synthetase from the Haloarchaeon Haloferax mediterranei
    • R.M. Martinez-Espinosa, J. Esclapez, V. Bautista, and M.J. Bonete An octameric prokaryotic glutamine synthetase from the Haloarchaeon Haloferax mediterranei FEMS Microbiol. Lett. 264 2006 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
  • 21
    • 0035976909 scopus 로고    scopus 로고
    • The story of glutamine synthetase regulation
    • E.R. Stadtman The story of glutamine synthetase regulation J. Biol. Chem. 276 2001 44357 44364
    • (2001) J. Biol. Chem. , vol.276 , pp. 44357-44364
    • Stadtman, E.R.1
  • 22
    • 0028308478 scopus 로고
    • Evolutionary relationships of bacterial and archaeal glutamine synthetase genes
    • J.R. Brown, Y. Masuchi, F.T. Robb, and W.F. Doolittle Evolutionary relationships of bacterial and archaeal glutamine synthetase genes J. Mol. Evol. 38 1994 566 576
    • (1994) J. Mol. Evol. , vol.38 , pp. 566-576
    • Brown, J.R.1    Masuchi, Y.2    Robb, F.T.3    Doolittle, W.F.4
  • 23
    • 0015980222 scopus 로고
    • Regulation of glutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors and l-glutamine
    • T.F. Deuel, and S. Prusiner Regulation of glutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors and l-glutamine J. Biol. Chem. 249 1974 257 264
    • (1974) J. Biol. Chem. , vol.249 , pp. 257-264
    • Deuel, T.F.1    Prusiner, S.2
  • 25
    • 11244263995 scopus 로고    scopus 로고
    • Complex formation and catalytic activation by the PII signaling protein of N-acetyl-l-glutamate kinase from Synechococcus elongates strain PCC 7942
    • M. Maheswaran, C. Urbanke, and K. Forchhammer Complex formation and catalytic activation by the PII signaling protein of N-acetyl-l-glutamate kinase from Synechococcus elongates strain PCC 7942 J. Biol. Chem. 279 2004 55202 55210
    • (2004) J. Biol. Chem. , vol.279 , pp. 55202-55210
    • Maheswaran, M.1    Urbanke, C.2    Forchhammer, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.