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HORT640 - Metabolic Plant Physiology
References, uridylyl
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Francis SH, Engleman EG. Cascade control of E. coli glutamine synthetase. I. Studies on the uridylyl transferase and uridylyl removing enzyme(s) from E. coli. Arch. Biochem. Biophys. 191: 590-601 (1978).
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).
Guranowski A, de Diego A, Sillero A, Gunther Sillero MA. Uridine 5'-polyphosphates (p4U and p5U) and uridine(5')polyphospho(5')nucleosides (Up(n)Ns) can be synthesized by UTP:glucose-1-phosphate uridylyltransferase from Saccharomyces cerevisiae. FEBS Lett. 561: 83-88 (2004).
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).
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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, 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, 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).
Jin LH, Um HJ, Yin CJ, Kim YH, Lee JH. Proteomic analysis of curdlan-producing Agrobacterium sp. in response to pH downshift. J. Biotechnol. 138: 80-87 (2008).
Johansson M, Nordlund S. Purification of P(II) and P(II)-UMP and in vitro studies of regulation of glutamine synthetase in Rhodospirillum rubrum. J. Bacteriol. 181: 6524-6529 (1999).
Johansson M, Nordlund S. Uridylylation of the P(II) protein in the photosynthetic bacterium Rhodospirillum rubrum. J. Bacteriol. 179: 4190-4194 (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).
Kalckar HM. 50 years of biological research--from oxidative phosphorylation to energy requiring transport regulation. Annu. Rev. Biochem. 60: 1-37 (1991).
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).
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).
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).
McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN Jr. Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana. Biochemistry 45: 3154-3162 (2006).
Mura U, Ceccherelli M, Gini S. In situ inactivation of E. coli uridylylation cycle is independent of the state of covalent modification of the components of the glutamine synthetase cascade. Arch. Biochem. Biophys. 219: 366-370 (1982).
Mura U, Stadtman ER. Glutamine synthetase adenylylation in permeabilized cells of Escherichia coli. J. Biol. Chem. 256: 13014-13021 (1981).
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).
Nolden L, Farwick M, Kramer R, Burkovski A. Glutamine synthetases of Corynebacterium glutamicum: transcriptional control and regulation of activity. FEMS Microbiol. Lett. 201: 91-98 (2001).
Read R, Pashley CA, Smith D, Parish T. The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis. Tuberculosis (Edinb.) 87: 384-390 (2007).
Reuther J, Wohlleben W. Nitrogen metabolism in Streptomyces coelicolor: transcriptional and post-translational regulation. J. Mol. Microbiol. Biotechnol. 12: 139-146 (2007).
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).
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).
Schluter A, Nohlen M, Kramer M, Defez R, Priefer UB. The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation. Microbiology 146: 2987-2996 (2000).
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).
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).
Stadtman ER, Hohman RJ, Davis JN, Wittenberger M, Chock PB, Rhee SG. Subunit interaction of adenylylated glutamine synthetase. Mol. Biol. Biochem. Biophys. 32: 144-156 (1980).
Strosser J, Ludke A, Schaffer S, Kramer R, Burkovski A. Regulation of GlnK activity: modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum. Mol. Microbiol. 54: 132-147 (2004).
Trippe R, Richly H, Benecke BJ. Biochemical characterization of a U6 small nuclear RNA-specific terminal uridylyltransferase. Eur. J. Biochem. 270: 971-980 (2003).
Van Dommelen A, Keijers V, Somers E, Vanderleyden J. Cloning and characterisation of the Azospirillum brasilense glnD gene and analysis of a glnD mutant. Mol. Genet. Genomics 266: 813-820 (2002).
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).
Varon-Castellanos R, Havsteen BH, Garcia-Moreno M, Valero-Ruiz E, Molina-Alarcon M, Garcia-Canovas F. Time course of the uridylylation and adenylylation states in the glutamine synthetase bicyclic cascade. Biochem. J. 294: 813-819 (1993).
Zhang Y, Pohlmann EL, Roberts GP. GlnD is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. J. Bacteriol. 187: 1254-1265 (2005).
Number of references = 79
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