Regulation of the Escherichia coli biosynthetic ornithine decarboxylase activity by phosphorylation and nucleotides

Anagnostopoulos, C; Kyriakidis, Dimitrios A.

doi:10.1016/s0167-4838(96)00107-0

Cited by 10 publications

(10 citation statements)

References 21 publications

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“…The accumulation of ppGpp leads to the cessation of stable RNA synthesis and appears to have a bearing on the fidelity of protein synthesis [36]. Treating recombinant ODC with calf intestine alkaline phosphatase leads to inactivation of ODC that can be allosterically reversed only by guanosyl or uridyl phosphate analogues at a concentration of 10 -4 or 10 -3 M [37]. Nucleotides are effective in activating ODC, in the order (G,U)TP>(G,U)DP>(G,U)MP.…”

Section: Reviewmentioning

confidence: 99%

“…[8- 3 H]GTP binds specifically to ODC since cold GTP but not ATP can dissociate the radioactive analogue. High concentration of GTP can dissociate the ODC-Az complex and either reactivate or liberate ODC [37]. …”

Section: Reviewmentioning

confidence: 99%

“…Biosynthetic ODC of E. coli can be phosphorylated both in vivo as well as in vitro [37]. An ODC-phosphorylating kinase was purified from middle-log growing E. coli K-12 strain MG1655, containing plasmid pODC [38].…”

Section: Reviewmentioning

confidence: 99%

“…In the autoradiogram one radioactive band appeared at 82 kDa, corresponding to the M r of the subunit of the biosynthetic ODC [37]. …”

Section: Reviewmentioning

confidence: 99%

“…The in vitro phosphorylation of ODC depends on the state of phosphorylation of the ODC molecule [37]. Therefore, the difficulties of the negative data on the ODC phosphorylation in different bacterial systems can be explained by the above observation.…”

Section: Reviewmentioning

confidence: 99%

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The role of bacterial antizyme: From an inhibitory protein to AtoC transcriptional regulator

Lioliou

Kyriakidis

2004

Microb Cell Fact

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This review considers the role of bacterial antizyme in the regulation of polyamine biosynthesis and gives new perspectives on the involvement of antizyme in other significant cellular mechanisms. Antizyme is a protein molecule induced by the end product of the enzymic reaction that it inhibits, in a non-competitive manner. The bacterial ornithine decarboxylase is regulated by nucleotides, phosphorylation and antizyme. The inhibition of ornithine decarboxylase by antizyme can be relieved to different degrees by DNA or by a variety of synthetic nucleic acid polymers, attributed to a specific interaction between nucleic acid and antizyme. Recently, this interplay between bacterial antizyme and nucleic acid was determined by discerning an additional function to antizyme that proved to be the atoC gene product, encoding the response regulator of the bacterial twocomponent system AtoS-AtoC. The gene located just upstream of atoC encodes the sensor kinase, named AtoS, that modulates AtoC activity. AtoC regulates expression of atoDAEB operon which is involved in short-chain fatty acid metabolism. Antizyme is thus referred to as AtoC, functioning both as a post-translational and transcriptional regulator. Also, the AtoS-AtoC signal transduction system in E. coli has a positive regulatory role on poly-(R)-3-hydroxybutyrate biosynthesis. The properties and gene structural similarities of antizymes from different organisms were compared. It was revealed that conserved domains are present mostly in the C-domain of all antizymes. BLAST analysis of the E. coli antizyme protein (AtoC) showed similarities around 69-58% among proteobacteria, g-proteobacteria, enterobacteria and the thermophilic bacterium Thermus thermophilus. A working hypothesis is proposed for the metabolic role of antizyme (AtoC) describing the significant biological implications of this protein molecule. Whether antizymes exist to other enzymes in different tissues, meeting the criteria discussed in the text remains to be elucidated. ReviewIn 1978 Seymour Cohen, the father of the field of polyamines posed the question "what do the polyamines do?" in his excellent article [1]. Since then, thousands of papers appeared in the literature concerning the metabolic role of polyamines. We will not attempt to discuss all the recent progress in the field, which has been well documented in book form [2][3][4][5][6][7][8] as well as in a number of excellent reviews [9][10][11][12][13][14][15]. Instead, we shall only consider the role of antizyme (Az) in the regulation of ornithine decarboxylase (L-ornithine carboxylyase, EC 4.1.1.17, ODC), its involvement in the bacterial two-component signal transduction system AtoS-AtoC [16], as well as its implication in other significant cellular functions.

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Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

“…In the autoradiogram one radioactive band appeared at 82 kDa, corresponding to the M r of the subunit of the biosynthetic ODC [37]. …”

Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

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The role of bacterial antizyme: From an inhibitory protein to AtoC transcriptional regulator

Lioliou

Kyriakidis

2004

Microb Cell Fact

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Signal transduction and adaptive regulation through bacterial two-component systems: the Escherichia coli AtoSC paradigm

Kyriakidis

Tiligada

2009

Amino Acids

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Adaptive signal transduction within microbial cells involves a multi-faceted regulated phosphotransfer mechanism that comprises structural rearrangements of sensor histidine kinases upon ligand-binding and phosphorylation-induced conformational changes in response regulators of versatile two-component systems (TCS), arisen early in bacterial evolution. In Escherichia coli, cross-talk between the AtoS histidine kinase and the AtoC response regulator, forming the AtoSC TCS, through His --> Asp phosphotransfer, activates AtoC directly to induce atoDAEB operon expression, thus modulating diverse fundamental cellular processes such as short-chain fatty acid catabolism, poly-(R)-3-hydroxybutyrate biosynthesis and chemotaxis. Among the inducers hitherto identified, acetoacetate is the classical activator. The AtoSC TCS functional modulation by polyamines, histamine and Ca(2+), as well as the role of AtoC as transcriptional regulator, add new promising perspectives in the physiological significance and potential pharmacological exploitation of this TCS in cell proliferation, bacteria-host interactions, chemotaxis, and adaptation.

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Phosphorylation activity of the response regulator of the two-component signal transduction system AtoS–AtoC in E. coli

Lioliou

Mimitou

Grigoroudis

et al. 2005

Biochimica et Biophysica Acta (BBA) - General Subjects

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Regulation of the Escherichia coli biosynthetic ornithine decarboxylase activity by phosphorylation and nucleotides

Cited by 10 publications

References 21 publications

The role of bacterial antizyme: From an inhibitory protein to AtoC transcriptional regulator

The role of bacterial antizyme: From an inhibitory protein to AtoC transcriptional regulator

Signal transduction and adaptive regulation through bacterial two-component systems: the Escherichia coli AtoSC paradigm

Phosphorylation activity of the response regulator of the two-component signal transduction system AtoS–AtoC in E. coli

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