메뉴 건너뛰기




Volumn 194, Issue 8, 2012, Pages 643-652

Uridylylation of herbaspirillum seropedicae glnb and glnk proteins is differentially affected by ATP, ADP and 2-oxoglutarate in vitro

Author keywords

GlnB; GlnK; Herbaspirillum seropedicae.; PII proteins; Uridylylation

Indexed keywords

2 OXOGLUTARIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; BACTERIAL PROTEIN; PROTEIN GLNB; PROTEIN GLND; PROTEIN GLNK; UNCLASSIFIED DRUG; URIDINE PHOSPHATE;

EID: 84866000515     PISSN: 03028933     EISSN: 1432072X     Source Type: Journal    
DOI: 10.1007/s00203-012-0799-9     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0035105144 scopus 로고    scopus 로고
    • PII signal transduction proteins, pivotal players in microbial nitrogen control
    • Arcondéguy T, Jack R, 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
  • 2
    • 0032895784 scopus 로고    scopus 로고
    • Characterization of the GlnK protein of Escherichia coli
    • Atkinson MR, Ninfa AJ (1999) Characterization of the GlnK protein of Escherichia coli. Mol Microbiol 32:301-313
    • (1999) Mol Microbiol , vol.32 , pp. 301-313
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 3
    • 0028061944 scopus 로고
    • Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator i (NRI or NtrC
    • Atkinson MR, Kamberov ES, Weiss RE, Ninfa AJ (1994) Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC). J Biol Chem 269:28288-28293
    • (1994) J Biol Chem , vol.269 , pp. 28288-28293
    • Atkinson, M.R.1    Kamberov, E.S.2    Weiss, R.E.3    Ninfa, A.J.4
  • 4
    • 0022629490 scopus 로고
    • Characterization of Herbaspirillum seropedicae gen. nov., sp. nov., a rootassociated nitrogen-fixing bacterium
    • Baldani JI, Baldani VLD, Seldin L, Döbereiner J (1986) Characterization of Herbaspirillum seropedicae gen. nov., sp. nov., a rootassociated nitrogen-fixing bacterium. Int J Syst Bacteriol 36:86-93
    • (1986) Int J Syst Bacteriol , vol.36 , pp. 86-93
    • Baldani, J.I.1    Vld, B.2    Seldin, L.3    Döbereiner, J.4
  • 5
    • 0030746346 scopus 로고    scopus 로고
    • Evidences for two possible glnB-type genes in Herbaspirillum seropedicae
    • Benelli EM, Souza EM, Funayama S, Rigo LU, Pedrosa FO (1997) Evidences for two possible glnB-type genes in Herbaspirillum seropedicae. J Bacteriol 179:4623-4626
    • (1997) J Bacteriol , vol.179 , pp. 4623-4626
    • Benelli, E.M.1    Souza, E.M.2    Funayama, S.3    Rigo, L.U.4    Pedrosa, F.O.5
  • 8
    • 34548444161 scopus 로고    scopus 로고
    • Purification and characterization of the bifunctional uridylyltransferase and the signal transducing proteins GlnB and GlnK from Herbaspirillum seropedicae
    • Bonatto AC, Couto GH, Souza EM, Arau'jo LM, Pedrosa FO, Noindorf L, Benelli EM (2007) Purification and characterization of the bifunctional uridylyltransferase and the signal transducing proteins GlnB and GlnK from Herbaspirillum seropedicae. Prot Expr Purif 55:293-299
    • (2007) Prot Expr Purif , vol.55 , pp. 293-299
    • Bonatto, A.C.1    Couto, G.H.2    Souza, E.M.3    Arau'Jo, L.M.4    Pedrosa, F.O.5    Noindorf, L.6    Benelli, E.M.7
  • 10
    • 33846641311 scopus 로고    scopus 로고
    • The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel
    • Conroy MJ, Durand A, Lupo D, Li X, Bullough PA, Winkler FK, Merrick M (2007) The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel. Proc Natl Acad Sci USA 104:1213-1218
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1213-1218
    • Conroy, M.J.1    Durand, A.2    Lupo, D.3    Li, X.4    Bullough, P.A.5    Winkler, F.K.6    Merrick, M.7
  • 11
    • 0037083882 scopus 로고    scopus 로고
    • Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB
    • Coutts G, Thomas G, Blakey D, 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
  • 12
    • 39049106044 scopus 로고    scopus 로고
    • P(II) signal transducers: Novel functional and structural insights
    • Forchhammer K (2008) P(II) signal transducers: novel functional and structural insights. Trends Microbiol 16:65-72
    • (2008) Trends Microbiol , vol.16 , pp. 65-72
    • Forchhammer, K.1
  • 13
    • 0028011762 scopus 로고
    • The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status
    • Forchhammer K, Tandeau De Marsac N (1994) The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status. J Bacteriol 176:84-91
    • (1994) J Bacteriol , vol.176 , pp. 84-91
    • Forchhammer, K.1    Tandeau De Marsac, N.2
  • 14
    • 33846106811 scopus 로고    scopus 로고
    • Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A
    • Gruswitz F, O'Connell J III, Stroud RM (2007) Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A . Proc Natl Acad Sci USA 104:42-47
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 42-47
    • Gruswitz, F.1    O'Connell Iii, J.2    Stroud, R.M.3
  • 15
    • 33645089445 scopus 로고    scopus 로고
    • ADP-ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB-dependent membrane sequestration of DraG
    • Huergo LF, Souza EM, Araujo MS, Pedrosa FO, Chubatsu LS, Steffens MBR, Merrick M (2006) ADP-ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB-dependent membrane sequestration of DraG. Mol Microbiol 59:326-337
    • (2006) Mol Microbiol , vol.59 , pp. 326-337
    • Huergo, L.F.1    Souza, E.M.2    Araujo, M.S.3    Pedrosa, F.O.4    Chubatsu, L.S.5    Mbr, S.6    Merrick, M.7
  • 16
    • 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 LF, Merrick M, Pedrosa FO, Chubatsu LS, Araujo LM, Souza EM (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
  • 17
    • 65449142921 scopus 로고    scopus 로고
    • In vitro interactions between the PII proteins and the nitrogenase regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase (DraT) and dinitrogenase reductase-activating glycohydrolase (DraG) in Azospirillum brasilense
    • Huergo LF, Merrick M, Monteiro RA, Chubatsu LS, Steffens MBR, Pedrosa FO, Souza EM (2009) In vitro interactions between the PII proteins and the nitrogenase regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase (DraT) and dinitrogenase reductase-activating glycohydrolase (DraG) in Azospirillum brasilense. J Biol Chem 284:6674-6682
    • (2009) J Biol Chem , vol.284 , pp. 6674-6682
    • Huergo, L.F.1    Merrick, M.2    Monteiro, R.A.3    Chubatsu, L.S.4    Mbr, S.5    Pedrosa, F.O.6    Souza, E.M.7
  • 19
    • 0030880188 scopus 로고    scopus 로고
    • The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction
    • Jaggi R, Van Heeswijk WC, Westerhoff HV, Ollis DL, Vasudevan SG (1997) The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J 16:5562-5571
    • (1997) EMBO J , vol.16 , pp. 5562-5571
    • Jaggi, R.1    Van Heeswijk, W.C.2    Westerhoff, H.V.3    Ollis, D.L.4    Vasudevan, S.G.5
  • 21
    • 36048991815 scopus 로고    scopus 로고
    • Escherichia coli PII signal transduction protein controlling nitrogen assimilation acts as a sensor of adenylate energy charge in vitro
    • Jiang P, Ninfa AJ (2007) Escherichia coli PII signal transduction protein controlling nitrogen assimilation acts as a sensor of adenylate energy charge in vitro. Biochemistry 46:12979-12996
    • (2007) Biochemistry , vol.46 , pp. 12979-12996
    • Jiang, P.1    Ninfa, A.J.2
  • 22
    • 73149108222 scopus 로고    scopus 로고
    • Sensation and signaling of alpha-ketoglutarate and adenylylate energy charge by the Escherichia coli PII signal transduction protein require cooperation of the three ligand-binding sites within the PII trimer
    • Jiang P, Ninfa AJ (2009) Sensation and signaling of alpha-ketoglutarate and adenylylate energy charge by the Escherichia coli PII signal transduction protein require cooperation of the three ligand-binding sites within the PII trimer. Biochemistry 48:11522-11531
    • (2009) Biochemistry , vol.48 , pp. 11522-11531
    • Jiang, P.1    Ninfa, A.J.2
  • 23
    • 0032530304 scopus 로고    scopus 로고
    • Enzymological characterization of the signal- transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein
    • Jiang P, Peliska JA, Ninfa AJ (1998) Enzymological characterization of the signal- transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein. Biochemistry 37:12782-12794
    • (1998) Biochemistry , vol.37 , pp. 12782-12794
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 24
    • 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 a-ketoglutarate
    • Jiang P, Mayo AE, Ninfa AJ (2007) Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and a-ketoglutarate. Biochemistry 46:4133-4146
    • (2007) Biochemistry , vol.46 , pp. 4133-4146
    • Jiang, P.1    Mayo, A.E.2    Ninfa, A.J.3
  • 25
    • 0029051027 scopus 로고
    • The Escherichia PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP
    • Kamberov ES, Atkinson MR, Ninfa AJ (1995) The Escherichia PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J Biol Chem 270:17797-17807
    • (1995) J Biol Chem , vol.270 , pp. 17797-17807
    • Kamberov, E.S.1    Atkinson, M.R.2    Ninfa, A.J.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T7
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T7. Nature 277:680-685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0028891890 scopus 로고
    • Activation of the dephosphorylation of nitrogen regulator I-phosphate of Escherichia coli
    • Liu J, Magasanik B (1995) Activation of the dephosphorylation of nitrogen regulator I-phosphate of Escherichia coli. J Bacteriol 177:926-931
    • (1995) J Bacteriol , vol.177 , pp. 926-931
    • Liu, J.1    Magasanik, B.2
  • 28
    • 15744405123 scopus 로고    scopus 로고
    • PII signal transduction proteins: Sensors of alpha-ketoglutarate that regulate nitrogen metabolism
    • Ninfa AJ, Jiang P (2005) PII signal transduction proteins: sensors of alpha-ketoglutarate that regulate nitrogen metabolism. Curr Opin Microbiol 8:168-173
    • (2005) Curr Opin Microbiol , vol.8 , pp. 168-173
    • Ninfa, A.J.1    Jiang, P.2
  • 32
    • 79957974830 scopus 로고    scopus 로고
    • Genome of Herbaspirillum seropedicae strain SmR1, a specialized diazotrophic endophyte of tropical grasses
    • Pedrosa FO, Monteiro RA, Wassem R, Cruz LM et al (2011) Genome of Herbaspirillum seropedicae strain SmR1, a specialized diazotrophic endophyte of tropical grasses. PLoS Genet 7:e1002064
    • (2011) PLoS Genet , vol.7
    • Pedrosa, F.O.1    Monteiro, R.A.2    Wassem, R.3    Cruz, L.M.4
  • 33
    • 0037312799 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein
    • Pioszak AA, Ninfa AJ (2003) Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein. J Bacteriol 185:1299-1315
    • (2003) J Bacteriol , vol.185 , pp. 1299-1315
    • Pioszak, A.A.1    Ninfa, A.J.2
  • 34
    • 77957281357 scopus 로고    scopus 로고
    • Control of AmtBGlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate
    • Radchenko MV, Thornton J, Merrick M (2010) Control of AmtBGlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate. J Biol Chem 285:31037-31045
    • (2010) J Biol Chem , vol.285 , pp. 31037-31045
    • Radchenko, M.V.1    Thornton, J.2    Merrick, M.3
  • 35
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 36
    • 0023664544 scopus 로고
    • Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene
    • Son HS, Rhee SG (1987) Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene. J Biol Chem 262:8690-8695
    • (1987) J Biol Chem , vol.262 , pp. 8690-8695
    • Son, H.S.1    Rhee, S.G.2
  • 37
    • 0025816153 scopus 로고
    • Sequence and structural organization of a nifA-like gene and part of a nifB-like gene of Herbaspirillum seropedicae strain Z78
    • Souza EM, Funayama S, Rigo LU, Yates MG, Pedrosa FO (1991) Sequence and structural organization of a nifA-like gene and part of a nifB-like gene of Herbaspirillum seropedicae strain Z78. J Gen Microbiol 137:1511-1522
    • (1991) J Gen Microbiol , vol.137 , pp. 1511-1522
    • Souza, E.M.1    Funayama, S.2    Rigo, L.U.3    Yates, M.G.4    Pedrosa, F.O.5
  • 38
    • 51149095176 scopus 로고    scopus 로고
    • Interaction of the signal transduction protein GlnJ with the cellular targets AmtB1, GlnE and GlnD in Rhodospirillum rubrum: Dependence on manganese, 2-oxoglutarato and the ADP/ATP ratio
    • Teixeira PF, Jonsson A, Frank M, Wang H, Nordlund S (2008) Interaction of the signal transduction protein GlnJ with the cellular targets AmtB1, GlnE and GlnD in Rhodospirillum rubrum: dependence on manganese, 2-oxoglutarato and the ADP/ATP ratio. Microbiology 154:2336-2347
    • (2008) Microbiology , vol.154 , pp. 2336-2347
    • Teixeira, P.F.1    Jonsson, A.2    Frank, M.3    Wang, H.4    Nordlund, S.5
  • 39
    • 34547799020 scopus 로고    scopus 로고
    • Membrane sequestration of PII proteins and nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus
    • Tremblay PL, Drepper T, Masepohl B, Hallenbeck PC (2007) Membrane sequestration of PII proteins and nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus. J Bacteriol 189:5850-5859
    • (2007) J Bacteriol , vol.189 , pp. 5850-5859
    • Tremblay, P.L.1    Drepper, T.2    Masepohl, B.3    Hallenbeck, P.C.4
  • 42
    • 0345353513 scopus 로고
    • Phosphorylation of nitrogen regulator i (NRI) of Escherichia coli
    • Weiss V, Magasanik B (1988) Phosphorylation of nitrogen regulatori (NRI) of Escherichia coli Proc Natl Acad Sci USA 858919-8923
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8919-8923
    • Weiss, V.1    Magasanik, B.2
  • 43
    • 34948865752 scopus 로고    scopus 로고
    • Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum
    • Wolfe DM, Zhang Y, Roberts GP (2007) Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum. J Bacteriol 189:6861-6869
    • (2007) J Bacteriol , vol.189 , pp. 6861-6869
    • Wolfe, D.M.1    Zhang, Y.2    Roberts, G.P.3
  • 44
    • 0032508415 scopus 로고    scopus 로고
    • GlnK, a PII-homologue: Structure revealsATP binding site and indicates how the T-loops may be involved in molecular recognition
    • XuY, Cheah E, Carr PD, van HeeswijkWC, WesterhoffHV, Vasudevan SG, OllisDL(1998) GlnK, a PII-homologue: structure revealsATP binding site and indicates how the T-loops may be involved in molecular recognition. J Mol Biol 282:149-165
    • (1998) J Mol Biol , vol.282 , pp. 149-165
    • Xuy Cheah, E.1    Carr, P.D.2    Van Heeswijkwc Westerhoffhv3    Vasudevan, S.G.4    Ollis, D.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.