Adler SP, Purich D, Stadtman ER. Cascade control of Escherichia coli glutamine synthetase. Properties of the PII regulatory protein and the uridylyltransferase-uridylyl-removing enzyme. J. Biol. Chem. 250: 6264-6272 (1975).

Ahlfors R, Lang S, Overmyer K, Jaspers P, Brosche M, Tauriainen A, Kollist H, Tuominen H, Belles-Boix E, Piippo M, Inze D, Palva ET, Kangasjarvi J. Arabidopsis RADICAL-INDUCED CELL DEATH1 belongs to the WWE protein-protein interaction domain protein family and modulates abscisic acid, ethylene, and methyl jasmonate responses. Plant Cell 16: 1925-1937 (2004).

Aldehni MF, Forchhammer K. Analysis of a non-canonical NtcA-dependent promoter in Synechococcus elongatus and its regulation by NtcA and PII. Arch. Microbiol. 184: 378-386 (2006).

Amar M, Patriarca EJ, Manco G, Bernard P, Riccio A, Lamberti A, Defez R, Iaccarino M. Regulation of nitrogen metabolism is altered in a glnB mutant strain of Rhizobium leguminosarum. Mol. Microbiol. 11: 685-693 (1994).

Amon J, Brau T, Grimrath A, HanBler E, Hasselt K, Holler M, JeBberger N, Ott L, Szokol J, Titgemeyer F, Burkovski A. Nitrogen control in Mycobacterium smegmatis: nitrogen-dependent expression of ammonium transport and assimilation proteins depends on OmpR-type regulator GlnR. J. Bacteriol. 190: 7108-7116 (2008).

Andrade SL, Dickmanns A, Ficner R, Einsle O. Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc. Natl. Acad. Sci. U.S.A. 102: 14994-14999 (2005).

Arcondeguy T, Huez I, Tillard P, Gangneux C, de Billy F, Gojon A, Truchet G, Kahn D. The Rhizobium meliloti PII protein, which controls bacterial nitrogen metabolism, affects alfalfa nodule development. Genes Dev. 11: 1194-1206 (1997).

Atkinson MR, Blauwkamp TA, Ninfa AJ. Context-dependent functions of the PII and GlnK signal transduction proteins in Escherichia coli. J. Bacteriol. 184: 5364-5375 (2002).

Atkinson MR, Kamberov ES, Weiss RL, Ninfa AJ. 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).

Atkinson MR, Ninfa AJ. Characterization of Escherichia coli glnL mutations affecting nitrogen regulation. J. Bacteriol. 174: 4538-4548 (1992).

Atkinson MR, Ninfa AJ. Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol. Microbiol. 29: 431-447 (1998).

Atkinson MR, Ninfa AJ. Characterization of the GlnK protein of Escherichia coli. Mol. Microbiol. 32: 301-313 (1999).

Bancroft S, Rhee SG, Neumann C, Kustu S. Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium. J. Bacteriol. 134: 1046-1055 (1978).

Berberich MA. Catabolism and nitrogen control in Escherichia coli. Curr. Top. Cell Regul. 26: 491-502 (1985).

Blauwkamp TA, Ninfa AJ. Nac-mediated repression of the serA promoter of Escherichia coli. Mol. Microbiol. 45: 351-363 (2002).

Blauwkamp TA, Ninfa AJ. Physiological role of the GlnK signal transduction protein of Escherichia coli: survival of nitrogen starvation. Mol. Microbiol. 46: 203-214 (2002).

Blume A, Fitzen M, Benie AJ, Peters T. Specificity of ligand binding to yeast hexokinase PII studied by STD-NMR. Carbohydr. Res. 344: 1567-1574 (2009).

Brown MS, Segal A, Stadtman ER. Modulation of glutamine synthetase adenylylation and deadenylylation is mediated by metabolic transformation of the P II -regulatory protein. Proc. Natl. Acad. Sci. U.S.A. 68: 2949-2953 (1971).

Bueno R, Pahel G, Magasanik B. Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli. J. Bacteriol. 164: 816-822 (1985).

Burillo S, Luque I, Fuentes I, Contreras A. Interactions between the nitrogen signal transduction protein PII and N-acetyl glutamate kinase in organisms that perform oxygenic photosynthesis. J. Bacteriol. 186: 3346-3354 (2004).

Caban CE, Ginsburg A. Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties. Biochemistry 15: 1569-1580 (1976).

Chan CS, Guo L, Shih MC. Promoter analysis of the nuclear gene encoding the chloroplast glyceraldehyde-3-phosphate dehydrogenase B subunit of Arabidopsis thaliana. Plant Mol. Biol. 46: 131-141 (2001).

Cheah E, Carr PD, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL. Structure of the Escherichia coli signal transducing protein PII. Structure 2: 981-990 (1994).

Chen YM, Ferrar TS, Lohmeir-Vogel EM, Morrice N, Mizuno Y, Berenger B, Ng KK, Muench DG, Moorhead GB. The PII signal transduction protein of Arabidopsis thaliana forms an arginine regulated complex with plastid N-acetyl glutamate kinase. J. Biol. Chem. 281: 5726-5733 (2006).

Colnaghi R, Rudnick P, He L, Green A, Yan D, Larson E, Kennedy C. Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation. Microbiology 147: 1267-1276 (2001).

Connelly HM, Pelletier DA, Lu TY, Lankford PK, Hettich RL. Characterization of pII family (GlnK1, GlnK2, and GlnB) protein uridylylation in response to nitrogen availability for Rhodopseudomonas palustris. Anal. Biochem. 357: 93-104 (2006).

Coutts G, Thomas G, Blakey D, Merrick M. Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB. EMBO J. 21: 536-545 (2002).

de Mel VS, Kamberov ES, Martin PD, Zhang J, Ninfa AJ, Edwards BF. Preliminary X-ray diffraction analysis of crystals of the PII protein from Escherichia coli. J. Mol. Biol. 243: 796-798 (1994).

De Vos M, Jander G. Choice and no-choice assays for testing the resistance of A. thaliana to chewing insects. J. Vis. Exp. 15 pii: 683 (2008).

de Zamaroczy M, Delorme F, Elmerich C. Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol. Gen. Genet. 224: 421-430 (1990).

de Zamaroczy M, Paquelin A, Elmerich C. Functional organization of the glnB-glnA cluster of Azospirillum brasilense. J. Bacteriol. 175: 2507-2515 (1993).

de Zamaroczy M, Paquelin A, Peltre G, Forchhammer K, Elmerich C. Coexistence of two structurally similar but functionally different PII proteins in Azospirillum brasilense. J. Bacteriol. 178: 4143-4149 (1996).

Detsch C, Stulke J. Ammonium utilization in Bacillus subtilis: transport and regulatory functions of NrgA and NrgB. Microbiology (U.K.) 149: 3289-3297 (2003).

Edwards R, Merrick M. The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation. Mol. Gen. Genet. 247: 189-198 (1995).

Ehlers C, Grabbe R, Veit K, Schmitz RA. Characterization of GlnK(1) from Methanosarcina mazei strain Go1: Complementation of an Escherichia coli glnK mutant strain by GlnK(1). J. Bacteriol. 184: 1028-1040 (2002).

Ehlers C, Weidenbach K, Veit K, Forchhammer K, Schmitz RA. Unique mechanistic features of post-translational regulation of glutamine synthetase activity in Methanosarcina mazei strain Go1 in response to nitrogen availability. Mol. Microbiol. 55: 1841-1854 (2005).

Eisenhut M, Huege J, Schwarz D, Bauwe H, Kopka J, Hagemann M. Metabolome phenotyping of inorganic carbon limitation in cells of the wild type and photorespiratory mutants of the cyanobacterium Synechocystis sp. strain PCC 6803. Plant Physiol. 148: 2109-2120 (2008).

Ferrario-Mery S, Bouvet M, Leleu O, Savino G, Hodges M, Meyer C. Physiological characterisation of Arabidopsis mutants affected in the expression of the putative regulatory protein PII. Planta 223: 28-39 (2005).

Foor F, Reuveny Z, Magasanik B. Regulation of the synthesis of glutamine synthetase by the PII protein in Klebsiella aerogenes. Proc. Natl. Acad. Sci. U.S.A. 77: 2636-2640 (1980).

Forchhammer K. Global carbon/nitrogen control by PII signal transduction in cyanobacteria: from signals to targets. FEMS Microbiol. Rev. 28: 319-233 (2004).

Forchhammer K. Glutamine signalling in bacteria. Front. Biosci. 12: 358-370 (2007).

Forchhammer K, Hedler A. Phosphoprotein PII from cyanobacteria--analysis of functional conservation with the PII signal-transduction protein from Escherichia coli. Eur. J. Biochem. 244: 869-875 (1997).

Forchhammer K, Hedler A, Strobel H, Weiss V. Heterotrimerization of PII-like signalling proteins: implications for PII-mediated signal transduction systems. Mol. Microbiol. 33: 338-349 (1999).

Forchhammer K, Irmler A, Kloft N, Ruppert U. P-II signalling in unicellular cyanobacteria: analysis of redox-signals and energy charge. Physiol. Plant. 120: 51-56 (2004).

Forchhammer K, Tandeau de Marsac N. Functional analysis of the phosphoprotein PII (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942. J. Bacteriol. 177: 2033-2040 (1995).

Foster R, Thorner J, Martin GS. Nucleotidylation, not phosphorylation, is the major source of the phosphotyrosine detected in enteric bacteria. J. Bacteriol. 171: 272-279 (1989).

Garcia E, Bancroft S, Rhee SG, Kustu S. The product of a newly identified gene, glnF, is required for synthesis of glutamine synthetase in Salmonella. Proc. Natl. Acad. Sci. U.S.A. 74: 1662-1666 (1977).

Garcia E, Rhee SG. Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme. J. Biol. Chem. 258: 2246-2253 (1983).

Garcia-Dominguez M, Florencio FJ. Nitrogen availability and electron transport control the expression of glnB gene (encoding PII protein) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 35: 723-734 (1997).

Harrison MA, Keen JN, Findlay JB, Allen JF. Modification of a glnB-like gene product by photosynthetic electron transport in the cyanobacterium Synechococcus 6301. FEBS Lett. 264: 25-28 (1990).

He L, Soupene E, Ninfa A, Kustu S. Physiological role for the GlnK protein of enteric bacteria: relief of NifL inhibition under nitrogen-limiting conditions. J. Bacteriol. 180: 6661-6667 (1998).

Heinrich A, Woyda K, Brauburger K, Meiss G, Detsch C, Stulke J, Forchhammer K. Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis. J. Biol. Chem. 281: 34909-34917 (2006).

Hodges M. Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation. J. Exp. Bot. 53: 905-916 (2002).

Hsieh MH, Lam HM, van de Loo FJ, Coruzzi G. A PII-like protein in Arabidopsis: putative role in nitrogen sensing. Proc. Natl. Acad. Sci. U.S.A. 95: 13965-13970 (1998).

Huang YF, Jordan WR, Wing RA, Morgan PW. Gene expression induced by physical impedance in maize roots. Plant Mol. Biol. 37: 921-930 (1998).

Irmler A, Forchhammer K. A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803. Proc. Natl. Acad. Sci. U.S.A. 98: 12978-12983 (2001).

Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL, Vasudevan SG. The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16: 5562-5571 (1997).

Jaggi R, Ybarlucea W, Cheah E, Carr PD, Edwards KJ, Ollis DL, Vasudevan SG. The role of the T-loop of the signal transducing protein PII from Escherichia coli. FEBS Lett. 391: 223-228 (1996).

Javelle A, Severi E, Thornton J, Merrick M. Ammonium sensing in Escherichia coli: role of the ammonium transporter AmtB and AmtB-GlnK complex formation. J. Biol. Chem. 279: 8530-8538 (2004).

Jiang P, Atkinson MR, Srisawat C, Sun Q, Ninfa AJ. Functional dissection of the dimerization and enzymatic activities of Escherichia coli nitrogen regulator II and their regulation by the PII protein. Biochemistry 39: 13433-13449 (2000).

Jiang P, Mayo AE, Ninfa AJ. Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate. Biochemistry 46: 4133-4146 (2007).

Jiang P, Ninfa AJ. Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme. Biochemistry 48: 415-423 (2009).

Jiang P, Ninfa AJ. Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein. J. Bacteriol. 181: 1906-1911 (1999).

Jiang P, Ninfa AJ. Escherichia coli PII signal transduction protein controlling nitrogen assimilation acts as a sensor of adenylate energy charge in vitro. Biochemistry 46: 12979-12996 (2007).

Jiang P, Peliska JA, Ninfa AJ. Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli. Biochemistry 37: 12795-12801 (1998).

Jiang P, Peliska JA, Ninfa AJ. 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).

Jiang P, Peliska JA, Ninfa AJ. The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry 37: 12802-12810 (1998).

Jiang P, Pioszak AA, Ninfa AJ. Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli. Biochemistry 46: 4117-4132 (2007).

Jiang P, Zucker P, Atkinson MR, Kamberov ES, Tirasophon W, Chandran P, Schefke BR, Ninfa AJ. Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J. Bacteriol. 179: 4342-4353 (1997).

Jiang P, Zucker P, Ninfa AJ. Probing interactions of the homotrimeric PII signal transduction protein with its receptors by use of PII heterotrimers formed in vitro from wild-type and mutant subunits. J. Bacteriol. 179: 4354-4360 (1997).

Jonsson A, Nordlund S. In vitro studies of the uridylylation of the three PII protein paralogs from Rhodospirillum rubrum: the transferase activity of R. rubrum GlnD is regulated by alpha-ketoglutarate and divalent cations but not by glutamine. J. Bacteriol. 189: 3471-3478 (2007).

Jonsson A, Teixeira PF, Nordlund S. The activity of adenylyltransferase in Rhodospirillum rubrum is only affected by alpha-ketoglutarate and unmodified PII proteins, but not by glutamine, in vitro. FEBS J. 274: 2449-2460 (2007).

Kamberov ES, Atkinson MR, Chandran P, Ninfa AJ. Effect of mutations in Escherichia coli glnL (ntrB), encoding nitrogen regulator II (NRII or NtrB), on the phosphatase activity involved in bacterial nitrogen regulation. J. Biol. Chem. 269: 28294-28299 (1994).

Kamberov ES, Atkinson MR, Feng J, Chandran P, Ninfa AJ. Sensory components controlling bacterial nitrogen assimilation. Cell. Mol. Biol. Res. 40: 175-191 (1994).

Kamberov ES, Atkinson MR, Ninfa AJ. The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J. Biol. Chem. 270: 17797-17807 (1995).

Kim IH, Kwak SJ, Kang J, Park SC. Transcriptional control of the glnD gene is not dependent on nitrogen availability in Escherichia coli. Mol. Cells 8: 483-490 (1998).

Kloft N, Forchhammer K. Signal transduction protein PII phosphatase PphA is required for light-dependent control of nitrate utilization in synechocystis sp. strain PCC 6803. J. Bacteriol. 187: 6683-6690 (2005).

Kloft N, Rasch G, Forchhammer K. Protein phosphatase PphA from Synechocystis sp. PCC 6803: the physiological framework of PII-P dephosphorylation. Microbiology 151: 1275-1283 (2005).

Kobayashi M, Takatani N, Tanigawa M, Omata T. Posttranslational regulation of nitrate assimilation in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 187: 498-506 (2005).

Konno H, Nakato T, Nakashima S, Katoh K. Lygodium japonicum fern accumulates copper in the cell wall pectin. J. Exp. Bot. 56: 1923-1931 (2005).

Laurent S, Forchhammer K, Gonzalez L, Heulin T, Zhang CC, Bedu S. Cell-type specific modification of PII is involved in the regulation of nitrogen metabolism in the cyanobacterium Anabaena PCC 7120. FEBS Lett. 576: 261-265 (2004).

Lee HM, Flores E, Forchhammer K, Herrero A, Tandeau De Marsac N. Phosphorylation of the signal transducer PII protein and an additional effector are required for the PII-mediated regulation of nitrate and nitrite uptake in the Cyanobacterium synechococcus sp. PCC 7942. Eur. J. Biochem. 267: 591-600 (2000).

Lee HM, Flores E, Herrero A, Houmard J, Tandeau de Marsac N. A role for the signal transduction protein PII in the control of nitrate/nitrite uptake in a cyanobacterium. FEBS Lett. 427: 291-295 (1998).

Leigh JA, Dodsworth JA. Nitrogen regulation in Bacteria and Archaea. Annu. Rev. Microbiol. 61: 349-377 (2007).

Liang YY, de Zamaroczy M, Arsene F, Paquelin A, Elmerich C. Regulation of nitrogen fixation in Azospirillum brasilense Sp7: involvement of nifA, glnA and glnB gene products. FEMS Microbiol. Lett. 79: 113-119 (1992).

Lillo C. Signalling cascades integrating light-enhanced nitrate metabolism. Biochem. J. 415: 11-19 (2008).

Lintala M, Allahverdiyeva Y, Kidron H, Piippo M, Battchikova N, Suorsa M, Rintamaki E, Salminen TA, Aro EM, Mulo P. Structural and functional characterization of ferredoxin-NADP+-oxidoreductase using knock-out mutants of Arabidopsis. Plant J. 49: 1041-1052 (2007).

Little R, Colombo V, Leech A, Dixon R. Direct interaction of the NifL regulatory protein with the GlnK signal transducer enables the Azotobacter vinelandii NifL-NifA regulatory system to respond to conditions replete for nitrogen. J. Biol. Chem. 277: 15472-15481 (2002).

Little R, Reyes-Ramirez F, Zhang Y, van Heeswijk WC, Dixon R. Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and the PII regulatory protein. EMBO J. 19: 6041-6050 (2000).

Liu J, Magasanik B. Activation of the dephosphorylation of nitrogen regulator I-phosphate of Escherichia coli. J. Bacteriol. 177: 926-931 (1995).

Liu J, Magasanik B. The glnB region of the Escherichia coli chromosome. J. Bacteriol. 175: 7441-7449 (1993).

Llacer JL, Contreras A, Forchhammer K, Marco-Marín C, Gil-Ortiz F, Maldonado R, Fita I, Rubio V. The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine. Proc. Natl. Acad. Sci. U.S.A. 104: 17644-17649 (2007).

Magasanik B, Bueno R. The role of uridylyltransferase and PII in the regulation of the synthesis of glutamine synthetase in Escherichia coli. Curr. Top. Cell Regul. 27: 215-220 (1985).

Mangum JH, Magni G, Stadtman ER. Regulation of glutamine synthetase adenylylation and deadenylylation by the enzymatic uridylylation and deuridylylation of the PII regulatory protein. Arch. Biochem. Biophys. 158: 514-525 (1973).

Mao XJ, Huo YX, Buck M, Kolb A, Wang YP. Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli. Nucleic Acids Res. 35: 1432-1440 (2007).

Martin DE, Reinhold-Hurek B. Distinct roles of PII-like signal transmitter proteins and amtB in regulation of nif gene expression, nitrogenase activity, and posttranslational modification of NifH in Azoarcus sp strain BH72. J. Bacteriol. 184: 2251-2259 (2002).

Michel-Reydellet N, Kaminski PA. Azorhizobium caulinodans PII and GlnK proteins control nitrogen fixation and ammonia assimilation. J. Bacteriol. 181: 2655-2658 (1999).

Mizuno Y, Berenger B, Moorhead GB, Ng KK. Crystal structure of Arabidopsis PII reveals novel structural elements unique to plants. Biochemistry 46: 1477-1483 (2007).

Mizuno Y, Moorhead GB, Ng KK. Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana. J. Biol. Chem. 282: 35733-35740 (2007).

Moorhead GB, Smith CS. Interpreting the plastid carbon, nitrogen, and energy status. A role for PII? Plant Physiol. 133: 492-498 (2003).

Moreno S, Patriarca EJ, Chiurazzi M, Meza R, Defez R, Lamberti A, Riccio A, Iaccarino M, Espin G. Phenotype of a Rhizobium leguminosarum ntrC mutant. Res. Microbiol. 143: 161-171 (1992).

Muro-Pastor MI, Reyes JC, Florencio FJ. Ammonium assimilation in cyanobacteria. Photosynth. Res. 83: 135-150 (2005).

Mutalik VK, Shah P, Venkatesh KV. Allosteric interactions and bifunctionality make the response of glutamine synthetase cascade system of Escherichia coli robust and ultrasensitive. J. Biol. Chem. 278: 26327-26332 (2003).

Ninfa AJ, Atkinson MR. PII signal transduction proteins. Trends Microbiol. 8: 172-179 (2000).

Ninfa AJ, Jiang P. PII signal transduction proteins: sensors of alpha-ketoglutarate that regulate nitrogen metabolism. Curr. Opin. Microbiol. 8: 168-173 (2005).

Ninfa AJ, Magasanik B. Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 83: 5909-5913 (1986).

Nualkaew N, De-Eknamkul W, Kutchan TM, Zenk MH. Membrane-bound geranylgeranyl diphosphate phosphatases: purification and characterization from Croton stellatopilosus leaves. Phytochemistry 67: 1613-1620 (2006).

Oliveira IC, Brenner E, Chiu J, Hsieh MH, Kouranov A, Lam HM, Shin MJ, Coruzzi G. Metabolite and light regulation of metabolism in plants: lessons from the study of a single biochemical pathway. Braz. J. Med. Biol. Res. 34: 567-575 (2001).

Ortega F, Acerenza L, Westerhoff HV, Mas F, Cascante M. Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades. Proc. Natl. Acad. Sci. U.S.A. 99: 1170-1175 (2002).

Osanai T, Sato S, Tabata S, Tanaka K. Identification of PamA as a PII-binding membrane protein important in nitrogen-related and sugar-catabolic gene expression in synechocystis sp. PCC 6803. J. Biol. Chem. 280: 34684-34690 (2005).

Pioszak AA, Jiang P, Ninfa AJ. The Escherichia coli PII signal transduction protein regulates the activities of the two-component system transmitter protein NRII by direct interaction with the kinase domain of the transmitter module. Biochemistry 39: 13450-13461 (2000).

Pioszak AA, Ninfa AJ. Mutations altering the N-terminal receiver domain of NRI (NtrC) that prevent dephosphorylation by the NRII-PII complex in Escherichia coli. J. Bacteriol. 186: 5730-5740 (2004).

Pioszak AA, Ninfa AJ. Mechanism of the PII-activated phosphatase activity of Escherichia coli NRII (NtrB): how the different domains of NRII collaborate to act as a phosphatase. Biochemistry 42: 8885-8899 (2003).

Pioszak AA, Ninfa AJ. 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).

Preger V, Scagliarini S, Pupillo P, Trost P. Identification of an ascorbate-dependent cytochrome b of the tonoplast membrane sharing biochemical features with members of the cytochrome b561 family. Planta 220: 365-375 (2005).

Ramsey JS, Jander G. Testing nicotine tolerance in aphids using an artificial diet experiment. J. Vis. Exp. 15 pii: 701 (2008).

Reuther J, Wohlleben W. Nitrogen metabolism in Streptomyces coelicolor: transcriptional and post-translational regulation. J. Mol. Microbiol. Biotechnol. 12: 139-146 (2007).

Reuveny Z, Foor F, Magasanik B. Regulation of glutamine synthetase by regulatory protein PII in Klebsiella aerogenes mutants lacking adenylyltransferase. J. Bacteriol. 146: 740-745 (1981).

Rhee SG, Chock PB. Purification and characterization of uridylylated and unuridylylated forms of regulatory protein PII involved in the glutamine synthetase regulation in Escherichia coli. Isozymes Curr. Top. Biol. Med. Res. 8: 141-153 (1983).

Rhee SG, Park SC, Koo JH. The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli. Curr. Top. Cell Regul. 27: 221-232 (1985).

Rietz S, Holk A, Scherer GF. Expression of the patatin-related phospholipase A gene AtPLA IIA in Arabidopsis thaliana is up-regulated by salicylic acid, wounding, ethylene, and iron and phosphate deficiency. Planta 219: 743-753 (2004).

Rudnick P, Kunz C, Gunatilaka MK, Hines ER, Kennedy C. Role of GlnK in NifL-mediated regulation of NifA activity in Azotobacter vinelandii. J. Bacteriol. 184: 812-820 (2002).

Shahollari B, Vadassery J, Varma A, Oelmuller R. A leucine-rich repeat protein is required for growth promotion and enhanced seed production mediated by the endophytic fungus Piriformospora indica in Arabidopsis thaliana. Plant J. 50: 1-13 (2007).

Shaltiel S, Adler SP, Purich D, Caban C, Senior P, Stadtman ER. Omega-aminoalkyl agaroses in the resolution of enzymes involved in regulation of glutamine metabolism. Proc. Natl. Acad. Sci. U.S.A. 72: 3397-3401 (1975).

Smith CS, Morrice NA, Moorhead GB. Lack of evidence for phosphorylation of Arabidopsis thaliana PII: implications for plastid carbon and nitrogen signaling. Biochim. Biophys. Acta 1699: 145-154 (2004).

Smith CS, Weljie AM, Moorhead GB. Molecular properties of the putative nitrogen sensor PII from Arabidopsis thaliana. Plant J. 33: 353-360 (2003).

Smith CS, Zaplachinski ST, Muench DG, Moorhead GB. Expression and purification of the chloroplast putative nitrogen sensor, PII, of Arabidopsis thaliana. Protein Expr. Purif. 25: 342-347 (2002).

Son HS, Rhee SG. 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).

Song Y, Peisach D, Pioszak AA, Xu Z, Ninfa AJ. Crystal structure of the C-terminal domain of the two-component system transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli. Biochemistry 43: 6670-6678 (2004).

Soulages JL, Kim K, Walters C, Cushman JC. Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean. Plant Physiol. 128: 822-832 (2002).

Starkenburg SR, Larimer FW, Stein LY, Klotz MG, Chain PS, Sayavedra-Soto LA, Poret-Peterson AT, Gentry ME, Arp DJ, Ward B, Bottomley PJ. Complete genome sequence of Nitrobacter hamburgensis X14 and comparative genomic analysis of species within the genus Nitrobacter. Appl. Environ. Microbiol. 74: 2852-2863 (2008).

Takatani N, Kobayashi M, Maeda S, Omata T. Regulation of nitrate reductase by non-modifiable derivatives of PII in the cells of Synechococcus elongatus strain PCC 7942. Plant Cell Physiol. 47: 1182-1186 (2006).

Takatani N, Omata T. Effects of PII deficiency on expression of the genes involved in ammonium utilization in the cyanobacterium Synechocystis sp. strain PCC 6803. Plant Cell Physiol. 47: 679-688 (2006).

Tanigawa R, Shirokane M, Maeda Si S, Omata T, Tanaka K, Takahashi H. Transcriptional activation of NtcA-dependent promoters of Synechococcus sp. PCC 7942 by 2-oxoglutarate in vitro. Proc. Natl. Acad. Sci. U.S.A. 99: 4251-4255 (2002).

Tate R, Mandrich L, Spinosa MR, Riccio A, Lamberti A, Iaccarino M, Patriarca EJ. The Rhizobium GstI protein reduces the NH4+ assimilation capacity of Rhizobium leguminosarum. Mol. Plant Microbe Interact. 14: 823-831 (2001).

Tate R, Riccio A, Merrick M, Patriarca EJ. The Rhizobium etli amtB gene coding for an NH4+ transporter is down-regulated early during bacteroid differentiation. Mol. Plant Microbe Interact. 11: 188-198 (1998).

Teplitski M, Chen H, Rajamani S, Gao M, Merighi M, Sayre RT, Robinson JB, Rolfe BG, Bauer WD. Chlamydomonas reinhardtii secretes compounds that mimic bacterial signals and interfere with quorum sensing regulation in bacteria. Plant Physiol. 134: 137-146 (2004).

Tikkanen M, Piippo M, Suorsa M, Sirpio S, Mulo P, Vainonen J, Vener AV, Allahverdiyeva Y, Aro EM. State transitions revisited - a buffering system for dynamic low light acclimation of Arabidopsis. Plant Mol. Biol. 62: 779-793 (2006).

Trumbly RJ. Glucose repression in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 6: 15-21 (1992).

van Heeswijk WC, Hoving S, Molenaar D, Stegeman B, Kahn D, Westerhoff HV. An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli. Mol. Microbiol. 21: 133-146 (1996).

van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9: 443-457 (1993).

van Heeswijk WC, Stegeman B, Hoving S, Molenaar D, Kahn D, Westerhoff HV. An additional PII in Escherichia coli: a new regulatory protein in the glutamine synthetase cascade. FEMS Microbiol. Lett. 132: 153-157 (1995).

van Heeswijk WC, Wen D, Clancy P, Jaggi R, Ollis DL, Westerhoff HV, Vasudevan SG. The Escherichia coli signal transducers PII (GlnB) and GlnK form heterotrimers in vivo: fine tuning the nitrogen signal cascade. Proc. Natl. Acad. Sci. U.S.A. 97: 3942-3947 (2000).

Xu Y, Carr PD, Huber T, Vasudevan SG, Ollis DL. The structure of the PII-ATP complex. Eur. J. Biochem. 268: 2028-2037 (2001).

Xu Y, Cheah E, Carr PD, van Heeswijk WC, Westerhoff HV, Vasudevan SG, Ollis DL. GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. J. Mol. Biol. 282: 149-165 (1998).

Xu YB, Wen DY, Clancy P, Carr PD, Ollis DL, Vasudevan SG. Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase. Protein Expr. Purif. 34: 142-146 (2004).

Zhang Y, Pohlmann EL, Conrad MC, Roberts GP. The poor growth of Rhodospirillum rubrum mutants lacking PII proteins is due to an excess of glutamine synthetase activity. Mol. Microbiol. 61: 497-510 (2006).

Zhang Y, Pu H, Wang Q, Cheng S, Zhao W, Zhang Y, Zhao J. PII is important in regulation of nitrogen metabolism but not required for heterocyst formation in the cyanobacterium Anabaena sp. PCC 7120. J. Biol. Chem. 282: 33641-33648 (2007).

Number of references = 148