Covalent modification of proteins in Escherichia coli growing anaerobically with nitrate as electron acceptor

Quentmeier, Armin

doi:10.1016/0378-1097(86)90359-9

Cited by 2 publications

(4 citation statements)

References 9 publications

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“…Covalent modification of proteins was demonstrated in various groups of aerobic as well as anaerobic bacteria [16,[19][20][21][22][23]. Protein phosphorylation in bacteria, hence, seems to play an important role in the regulation of enzyme activities involved in different metabolic pathways.…”

Section: Discussionmentioning

confidence: 99%

“…After incubation with RNase/DNase mixture (0.05 mg of each) for 15 min at 30 ° C, samples (50/~g of protein) were subjected to onedimensional SDS-gel electrophoresis (11.5%, w/v). Gels were fixed dried and autoradiographed as previously described [16,17]. For the two-dimensional gel electrophoresis aliquots of crude extracts (250/~g protein) were analyzed as described earlier [18,19].…”

Section: Kinase Assay and Protein Separationmentioning

confidence: 99%

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Covalent modification of proteins in Bacillus subtilis during the process of sporulation, germination and outgrowth

Köhler

Antranikian

1989

FEMS Microbiology Letters

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Cells of Bacillus subtilis 168+ were labeled with 32P-orthophosphate during the process of sporulation, germination and outgrowth. By two-dimensional gel electrophoresis, at least 30 protein species were found to be radioactively labeled; 30% of these were modified by phosphorylation. Significant changes in the protein phosphorylation pattern during growth and cellular differentiation could be demonstrated. Using gamma-32P-ATP evidence for an ATP-dependent protein kinase was also obtained. Under these conditions 4 proteins with a molecular mass of 109,600; 103,100; 73,300 and 32,200 Da were found to be phosphorylated.

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Section: Discussionmentioning

confidence: 99%

Section: Kinase Assay and Protein Separationmentioning

confidence: 99%

Covalent modification of proteins in Bacillus subtilis during the process of sporulation, germination and outgrowth

Köhler

Antranikian

1989

FEMS Microbiology Letters

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“…Using 32 P-phosphate it was shown that the activity of the ligase is regulated by covalent modification of the enzyme by phosphorylation and dephosphorylation [19]. Although various prokaryotic proteins have been shown to be phosphorylated [128][129][130][131][132][133][134][135][136][137], such a mechanism is only reported for few enzyme systems [19,138]. In the presence of citrate the ligase is activated by phosphorylation.…”

Section: Citrate Lyase Actiuationmentioning

confidence: 99%

“…The positive effect of L-glutamate on citrate lyase ligase suggests that this metabolite, which signals the presence of citrate, might influence this cascade system by favoring the phosphorylation of the ligase. The finding that other bacterial proteins are also phosphorylated [128][129][130][131][132][133][134][135][136][137] indicates that other enzyme systems might be regulated by related mechanisms. Unlike…”

Section: General Model Of Citrate Lyase Regulation In C Sphenoidesmentioning

confidence: 99%

Citrate metabolism in anaerobic bacteria

Antranikian

Giffhorn

1987

FEMS Microbiology Letters

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The regulation of anaerobic citrate metabolism is very diverse among different groups of bacteria. In organisms like Streptococcus lactis and Clostridium sporosphaeroides which lack citrate synthase, the activity of its antagonistic enzyme, citrate lyase, need not be regulated. Many anaerobes like Rhodocyclus gelatinosus and Clostridium sphenoides are able to synthesize their own l‐glutamate and contain citrate synthase. In these bacteria the activity of citrate metabolizing enzymes which are involved in a cascade system are under strict control. In Rc. gelatinosus activation/inactivation of citrate lyase is controlled by acetylation/deacetylation which is catalyzed by its corresponding regulatory enzymes, citrate lyase ligase and citrate lyase deacetylase. In C. sphenoides inactivation of citrate lyase is accomplished by deacetylation as well as by changing in the enzyme conformation. Activation of citrate lyase is catalyzed by citrate lyase ligase whose activity in addition is modulated by phosphorylation/dephosphorylation. Further, electron transport process also seems to play a role in the inactivation of citrate metabolizing enzymes in enteric bacteria.

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Covalent modification of proteins in Escherichia coli growing anaerobically with nitrate as electron acceptor

Cited by 2 publications

References 9 publications

Covalent modification of proteins in Bacillus subtilis during the process of sporulation, germination and outgrowth

Covalent modification of proteins in Bacillus subtilis during the process of sporulation, germination and outgrowth

Citrate metabolism in anaerobic bacteria

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