PII signal transduction proteins

Trends in Microbiology

Volumn 8, Issue 4, 2000, Pages 172-179

  Ninfa, Alexander J ^a   Atkinson, Mariette R ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE AMMONIA LIGASE; REGULATOR PROTEIN; SIGNAL PEPTIDE;

BACTERIAL METABOLISM; ESCHERICHIA COLI; METABOLISM; NITROGEN FIXATION; NITROGEN METABOLISM; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN CONFORMATION; REVIEW; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BACTERIA; BACTERIAL PROTEINS; CARBON; CARRIER PROTEINS; ESCHERICHIA COLI; EUKARYOTIC CELLS; MODELS, MOLECULAR; NITROGEN; PII NITROGEN REGULATORY PROTEINS; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

ARCHAEA; BACTERIA (MICROORGANISMS);

EID: 0034176532     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(00)01709-1     Document Type: Review

References (49)

1. Kaiser D. Cell fate and organogenesis in bacteria. Trends Genet. 15:1999;273-277.
2. Senior P.J. Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J. Bacteriol. 123:1975;407-418.
3. Shapiro B.M.et al. Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: a new form of the enzyme with altered regulatory and kinetic properties. Proc. Natl. Acad. Sci. U. S. A. 58:1967;642-649.
4. Ninfa A., 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. 83:1986;5909-5913.
5. Jiang P., Ninfa A.J. Regulation of the autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein. J. Bacteriol. 181:1999;1906-1911.
6. Mangum J.H.et al. Regulation of glutamine synthetase adenylylation and deadenylylation by the enzymatic uridylylation and deuridylylation of the PII regulatory protein. Arch. Biochem. Biophys. 158:1973;514-525.
7. Jiang P.et al. 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. 37:1998;12782-12794.
8. Atkinson M.R.et al. 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. 269:1994;28288-28293.
9. Kamberov E.S.et al. The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J. Biol. Chem. 270:1995;17797-17807.
10. Shapiro B.M. The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements. Biochemistry. 8:1969;659-670.
11. Liu J., Magasanik B. Activation of the dephosphorylation of nitrogen regulator I-phosphate of Escherichia coli. J. Bacteriol. 177:1995;926-931.
12. Jiang P.et al. Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli. Biochemistry. 37:1998;12795-12801.
13. Jiang P.et al. The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry. 37:1998;12802-12810.
14. van Heeswijk W.C.et al. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9:1993;443-457.
15. Reitzer L.J., Magasanik B. Isolation of the nitrogen assimilation regulator NRI, the product of the glnG gene of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 80:1983;5554-5558.
16. Atkinson M.R., Ninfa A.J. Mutational analysis of the bacterial signal-transducing protein kinase/phosphatase nitrogen regulator II (NRII or NtrB). J. Bacteriol. 175:1993;7016-7023.
17. Wong P-K.et al. In vitro transcription of the nitrogen fixation regulatory operon I of Klebsiella pneumoniae. J. Bacteriol. 169:1987;2876-2880.
18. Feng J.et al. Activation of transcription initiation from the nac promoter of Klebsiella aerogenes. J. Bacteriol. 177:1995;5523-5534.
19. van Heeswijk W.C.et al. An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli. Mol. Microbiol. 21:1996;133-146.
20. Atkinson M.R., Ninfa A.J. Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol. Microbiol. 29:1996;431-447.
21. Ninfa A.J.et al. Initiation of transcription at the bacterial glnAp2 promoter by purified E. coli components is facilitated by enhancers. Cell. 50:1997;1039-1046.
22. Wedel A.et al. A bacterial enhancer functions to tether a transcriptional activator near a promoter. Science. 248:1990;486-490.
23. Santero E.et al. Role of integration host factor in stimulating transcription from the σ54-dependent nifH promoter. J. Mol. Biol. 227:1992;602-620.
24. Feng J.et al. Repression of the Klebsiella aerogenes nac promoter. J. Bacteriol. 177:1995;5535-5538.
25. Shiau S.P.et al. Role of nitrogen regulator I (NtrC), the transcriptional activator of glnA in enteric bacteria, in reducing expression of glnA during nitrogen-limited growth. J. Bacteriol. 174:1992;179-185.
26. Atkinson M.R., Ninfa A.J. Characterization of the GlnK protein of Escherichia coli. Mol. Microbiol. 32:1999;301-313.
27. He L.et al. Physiological role for the GlnK protein of enteric bacteria: relief of NifL inhibition under nitrogen-limiting conditions. J. Bacteriol. 180:1998;6661-6667.
28. Jack R.et al. The signal transduction protein GlnK is required for NifL-dependent nitrogen control of nif gene expression in Klebsiella pneumoniae. J. Bacteriol. 181:1999;1156-1162.
29. Forchhammer K.et al. Heterotrimerization of PII-like signalling proteins: implications for PII-mediated signal transduction systems. Mol. Microbiol. 33:1999;338-349.
30. Liu J., Magasanik B. The glnB region of the Escherichia coli chromosome. J. Bacteriol. 175:1993;7441-7449.
31. Jakoby M.et al. Nitrogen regulation in Corynebacterium glutamicum: isolation of genes involved and biochemical characterization of corresponding proteins. FEMS Microbiol. Lett. 173:1999;303-310.
32. Colonna-Romano S.et al. Tight linkage of glnA and a putative regulatory gene in Rhizobium leguminosarum. Nucleic Acids Res. 15:1987;1951-1963.
33. Zinchenko V.et al. Nucleotide sequence and characterization of the Rhodobacter sphaeroides glnB and glnA genes. Microbiology. 140:1994;2143-2151.
34. De Zamaroczy M.et al. Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol. Gen. Genet. 224:1990;421-430.
35. Qian Y., Tabita F.R. Expression of glnB and a glnB-like gene (glnK) in a ribulose bisphosphate carboxylase/oxygenase-deficient mutant of Rhodobacter sphaeroides. J. Bacteriol. 180:1998;4644-4649.
36. Sibold L.et al. Nucleotide sequence of nifH regions from Methanobacterium ivanovii and Methanosarcina barkeri 227 and characterization of glnB-like genes. Res. Microbiol. 142:1991;5-12.
37. Wray L.V.et al. The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein. J. Bacteriol. 176:1994;108-114.
38. Forchhammer K., Tandeau de Marsac N. The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N status. J. Bacteriol. 176:1994;84-91.
39. Tsinoremas N.F.et al. Photosynthetic electron transport controls nitrogen assimilation in cyanobacteria by means of post-translational modification of the glnB gene product. Proc. Natl. Acad. Sci. U. S. A. 88:1991;4565-4569.
40. Forchhammer K., Tandeau de Marsac N. Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain 7942: analysis of in vitro kinase activity. J. Bacteriol. 177:1995;5812-5817.
41. Irmler A.et al. Dephosphorylation of the phosphoprotein PII in Synechococcus PCC 7942: identification of an ATP and 2-oxoglutarate-regulated phosphatase activity. Mol. Microbiol. 26:1997;81-90.
42. Reith M.E., Munholland J. Complete nucleotide sequence of the Porphyra purpurea chloroplast genome. Plant Mol. Biol. Rep. 13:1995;333-335.
43. Hsieh M.H.et al. A PII-like protein in Arabidopsis: putative role in nitrogen sensing. Proc. Natl. Acad. Sci. U. S. A. 95:1998;13965-13970.
44. Cheah E.et al. Structure of the Escherichia coli signal transduction protein PII. Structure. 2:1994;981-990.
45. Carr P.D.et al. X-ray structure of the signal transduction protein PII from Escherichia coli at 1.9 Å Acta Crystallog. 52:1996;93-104.
46. Xu Y.et al. GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. J. Mol. Biol. 282:1998;149-165.
47. 10-helix. Trends Biochem. Sci. 16:1991;350-353.
48. Jiang P.et al. Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J. Bacteriol. 179:1997;4342-4353.
49. Jiang P.et al. 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. 179:1997;4354-4360.