Influence of the ADP/ATP ratio, 2-oxoglutarate and divalent ions on Azospirillum brasilense PII protein signalling

Microbiology (United Kingdom)

Volumn 158, Issue 6, 2012, Pages 1656-1663

  Gerhardt, Edileusa C M ^a   Araújo, Luíza M ^a   Ribeiro, Ronny R ^b   Chubatsu, Leda S ^a   Scarduelli, Marcelo ^a   Rodrigues, Thiago E ^a   Monteiro, Rose A ^a   Pedrosa, Fábio O ^a   Souza, Emanuel M ^a   Huergo, Luciano F ^a  

^a FEDERAL UNIVERSITY OF PARANÁ   (Brazil)

^b UNIVERSIDADE TECNOLÓGICA FEDERAL DO PARANÁ   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMTB PROTEIN; BACTERIAL PROTEIN; CALCIUM ION; DRAG PROTEIN; DRAT PROTEIN; GLNB PROTEIN; GLNZ PROTEIN; MAGNESIUM ION; MANGANESE; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; AZOSPIRILLUM BRASILENSE; CONCENTRATION (PARAMETERS); IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AZOSPIRILLUM BRASILENSE; BACTERIAL PROTEINS; CATIONS, DIVALENT; GENE EXPRESSION REGULATION, BACTERIAL; KETOGLUTARIC ACIDS; PII NITROGEN REGULATORY PROTEINS; SIGNAL TRANSDUCTION;

AZOSPIRILLUM BRASILENSE; PROTEOBACTERIA;

EID: 84861885483     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.058446-0     Document Type: Article

References (33)

1. Araújo, M. S., Baura, V. A., Souza, E. M., Benelli, E. M., Rigo, L. U., Steffens, M. B., Pedrosa, F. O. & Chubatsu, L. S. (2004). In vitro uridylylation of the Azospirillum brasilense N-signal transducing GlnZ protein. Protein Expr Purif 33, 19-24.
2. Araújo, L. M., Huergo, L. F., Invitti, A. L., Gimenes, C. I., Bonatto, A. C., Monteiro, R. A., Souza, E. M., Pedrosa, F. O. & Chubatsu, L. S. (2008). Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein. Braz J Med Biol Res 41, 289-294.
3. Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J. & Rabinowitz, J. D. (2009). Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat Chem Biol 5, 593-599.
4. Bonatto, A. C., Souza, E. M., Oliveira, M. A., Monteiro, R. A., Chubatsu, L. S., Huergo, L. F. & Pedrosa, F. O. (2012). Uridylylation of Herbaspirillum seropedicae GlnB and GlnK proteins is differentially affected by ATP, ADP and 2-oxoglutarate in vitro. Arch Microbiol [Epub ahead of print].
5. Conroy, M. J., Durand, A., Lupo, D., Li, X. D., Bullough, P. A., Winkler, F. K. & Merrick, M. (2007). The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel. Proc Natl Acad Sci U S A 104, 1213-1218.
6. Zof Azospirillum brasilense provide intracellular signalling for selective regulation of various nitrogen-dependent functions. Mol Microbiol 29, 449-463.
7. Dixon, R. & Kahn, D. (2004). Genetic regulation of biological nitrogen fixation. Nat Rev Microbiol 2, 621-631.
8. Dodsworth, J. A. & Leigh, J. A. (2006). Regulation of nitrogenase by 2-oxoglutarate-reversible, direct binding of a PII-like nitrogen sensor protein to dinitrogenase. Proc Natl Acad Sci U S A 103, 9779-9784.
9. Dominguez, D. C. (2004). Calcium signalling in bacteria. Mol Microbiol 54, 291-297.
10. Fokina, O., Chellamuthu, V. R., Forchhammer, K. & Zeth, K. (2010). Mechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction protein. Proc Natl Acad Sci U S A 107, 19760-19765.
11. Fokina, O., Herrmann, C. & Forchhammer, K. (2011). Signaltransduction protein P(II) from Synechococcus elongatus PCC 7942 senses low adenylate energy charge in vitro. Biochem J 440, 147-156.
12. Forchhammer, K. (2008). P(II) signal transducers: novel functional and structural insights. Trends Microbiol 16, 65-72.
13. Harding, M. M. (2000). The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions. Acta Crystallogr D Biol Crystallogr 56, 857-867.
14. Huergo, L. F., Merrick, M., Pedrosa, F. O., Chubatsu, L. S., Araújo, L. M. & Souza, E. M. (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.
15. Huergo, L. F., Merrick, M., Monteiro, R. A., Chubatsu, L. S., Steffens, M. B., Pedrosa, F. O. & Souza, E. M. (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.
16. Huergo, L. F., Pedrosa, F. O., Muller-Santos, M., Chubatsu, L. S., Monteiro, R. A., Merrick, M. & Souza, E. M. (2012). PII signal transduction proteins: pivotal players in post-translational control of nitrogenase activity. Microbiology 158, 176-190.
17. Jiang, P. & Ninfa, A. J. (2009). Sensation and signaling of alphaketoglutarate and adenylylate energy charge by the Escherichia coli PII signal transduction protein require cooperation of the three ligandbinding sites within the PII trimer. Biochemistry 48, 11522-11531.
18. Jiang, P., Zucker, P., Atkinson, M. R., Kamberov, E. S., Tirasophon, W., Chandran, P., Schefke, B. R. & Ninfa, A. J. (1997). Structure/ function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J Bacteriol 179, 4342-4353.
19. Jiang, P., Peliska, J. A. & Ninfa, A. J. (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.
20. Leganés, F., Forchhammer, K. & Fernández-Piñas, F. (2009). Role of calcium in acclimation of the cyanobacterium Synechococcus elongatus PCC 7942 to nitrogen starvation. Microbiology 155, 25-34.
21. Maheswaran, M., Urbanke, C. & Forchhammer, K. (2004). Complex formation and catalytic activation by the PII signaling protein of Nacetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942. J Biol Chem 279, 55202-55210.
22. Maier, S., Schleberger, P., Lü, W., Wacker, T., Pflüger, T., Litz, C. & Andrade, S. L. (2011). Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing of 2-oxoglutarate. PLoS ONE 6, e26327.
23. Moure, V. R., Razzera, G., Araújo, L. M., Oliveira, M. A., Gerhardt, E. C., Müller-Santos, M., Almeida, F., Pedrosa, F. O., Valente, A. P. & other authors (2012). Heat stability of Proteobacterial PII protein facilitate purification using a single chromatography step. Protein Expr Purif 81, 83-88.
24. Paul, T. D. & Ludden, P. W. (1984). Adenine nucleotide levels in Rhodospirillum rubrum during switch-off of whole-cell nitrogenase activity. Biochem J 224, 961-969.
25. Radchenko, M. V., Thornton, J. & Merrick, M. (2010). Control of AmtB-GlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate. J Biol Chem 285, 31037-31045.
26. Rajendran, C., Gerhardt, E. C., Bjelic, S., Gasperina, A., Scarduelli, M., Pedrosa, F. O., Chubatsu, L. S., Merrick, M., Souza, E. M. & other authors (2011). Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction. Proc Natl Acad Sci U S A 108, 18972-18976.
27. Rodrigues, T. E., Souza, V. E., Monteiro, R. A., Gerhardt, E. C., Araújo, L. M., Chubatsu, L. S., Souza, E. M., Pedrosa, F. O. & Huergo, L. F. (2011). In vitro interaction between the ammonium transport protein AmtB and partially uridylylated forms of the P(II) protein GlnZ. Biochim Biophys Acta 1814, 1203-1209.
28. Sarkar, A., Köhler, J., Hurek, T. & Reinhold-Hurek, B. (2012). A novel regulatory role of the Rnf complex of Azoarcus sp. strain BH72. Mol Microbiol 83, 408-422.
29. Senior, P. J. (1975). Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J Bacteriol 123, 407-418.
30. Teixeira, P. F., 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-oxoglutarate and the ADP/ATP ratio. Microbiology 154, 2336-2347.
31. Truan, D., Huergo, L. F., Chubatsu, L. S., Merrick, M., Li, X. D. & Winkler, F. K. (2010). A new P(II) protein structure identifies the 2-oxoglutarate binding site. J Mol Biol 400, 531-539.
32. Upchurch, R. G. & Mortenson, L. E. (1980). In vivo energetics and control of nitrogen fixation: changes in the adenylate energy charge and adenosine 59-diphosphate/adenosine 59-triphosphate ratio of cells during growth on dinitrogen versus growth on ammonia. J Bacteriol 143, 274-284.
33. Xu, Y., Cheah, E., Carr, P. D., van Heeswijk, W. C., Westerhoff, H. V., Vasudevan, S. G. & Ollis, D. L. (1998). 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.