Methylation of a membrane protein involved in bacterial chemotaxis.

Kort, Edward N.; Goy, Michael F.; Larsen, Steven H.; Adler, Julius

doi:10.1073/pnas.72.10.3939

Cited by 222 publications

(150 citation statements)

References 29 publications

(21 reference statements)

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“…Data for the time course of methylation in § This appears to contradict previously published data which indicate that, following addition of an attractant, a transient rise and fall in the level of methylation occurs (13); however, in the earlier experiment the possibility that the decline in the level of methylation was due to metabolism of the attractant was not ruled out. In Fig.…”

Section: Methodscontrasting

confidence: 79%

“…Thus, it is important to bear in mind that although the bulk of the methylation shows the characteristics described below, nevertheless a minor component, represented by one or more bands, may differ significantly in its properties. RESULTS Previous publications have described the methylation of proteins in the cytoplasmic membrane of E. coli that are involved in chemotaxis (13,14,18). These proteins, collectively called MCP for methyl-accepting chemotaxis proteins, can be divided into two functional units, MCP I and MCP II, which are the products of different genes (14,18).…”

Section: Methodsmentioning

confidence: 97%

“…Upon removal of the attractant the level of methylation very rapidly falls to the basal value. Previously we have shown that adaptation requires methionine, but maintenance of the adapted state and de-adaptation do not [Springer, M. S., Coy, M. F. & Adler, J. (1975) Prc.…”

mentioning

confidence: 99%

“…Several years ago it was discovered that L-methionine is absolutely required for chemotaxis in E. coil (11). Subsequently it was shown that sensory adaptation involves a methionine-dependent process, but that maintenance of the adapted state and de-adaptation are both methionine-independent (12 had discovered that methionine serves as the methyl donor for a protein-methylation reaction that is involved in the chemotactic response (13). In this paper we demonstrate that the methylation reaction appears to regulate the state of adaptation of the cell.…”

mentioning

confidence: 99%

“…Bacteria. All experiments were performed with E. coli strain RP477 metF (13). This strain is chemotactically wild type and requires threonine, leucine, and histidine, as well as being metF.…”

mentioning

confidence: 99%

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Sensory transduction in Escherichia coli : Role of a protein methylation reaction in sensory adaptation

Goy

Springer²,

Adler³

1977

Proc. Natl. Acad. Sci. U.S.A.

194

119

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The behavioral response of Escherichia coli to the addition of a stimulatory compound is transient; thus the organism undergoes sensory adaptation. When the compound is removed, E. coli undergoes the inverse process, called deadaptation, and very rapidly regains its sensitivity to the stimulus. In this communication we demonstrate that the previously reported methylation of several cytoplasmic membrane proteins is correlated with, and very likely controls, the state of adaptation of the cell.In the absence of an added stimulus these proteins are methylated to a basal level. When the bacteria are stimulated by the addition of an attractant, the extent of methylation increases over a period of several minutes to a new level, which is maintained as long as the attractant is present. The magnitude of the increase in methylation is a function of the size of the stimulus and is directly proportional to the duration of the behavioral response.

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Section: Methodscontrasting

confidence: 79%

Section: Methodsmentioning

confidence: 97%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Sensory transduction in Escherichia coli : Role of a protein methylation reaction in sensory adaptation

Goy

Springer²,

Adler³

1977

Proc. Natl. Acad. Sci. U.S.A.

194

119

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Regulation of Macrophage Lysosomal Secretion by Adenosine, Adenosine Phosphate Esters, and Related Structural Analogues of Adenosine

Riches

Watkins

Henson

et al. 1985

Journal of Leukocyte Biology

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Zymosan particle-stimulated beta-galactosidase secretion by mouse peritoneal macrophages was found to be inhibited by micromolar concentrations of adenosine, AMP, ADP, and ATP. Inhibition by all four agents was increased to approximately 80% by adding erythro-9-(2-hydroxy-3-nonyl) adenine (EHNA; 10 microM) an adenosine deaminase inhibitor, to the incubation medium. The inhibition of lysosomal enzyme secretion by ATP, ADP, and AMP was reversed by adding alpha, beta -methylene ADP (100 microM), a 5'-nucleotidase inhibitor, to the incubation medium. Inhibition by adenosine, however, was unaffected by alpha, beta -methylene ADP indicating that the inhibition by AMP, ADP, and ATP only occurred after they had been converted to adenosine by cell surface phosphohydrolases, including 5'-nucleotidase. Theophylline, a competitive antagonist of the binding of adenosine to plasma membrane adenosine receptors, failed to reverse the inhibitory effect of adenosine indicating the probable site of adenosine action to be intracellular. Other purine nucleosides, e.g., guanosine, and several purine and ribosemodified structural analogues of adenosine also inhibited zymosan-stimulated beta-galactosidase secretion, while xanthosine and certain pyrimidine nucleosides, e.g., thymidine, were inactive in this respect.

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The involvement of methyl transfer reactions and S‐adenosylhomocysteine in the regulation of bovine sperm motility

Goh

Hoskins

1985

Gamete Research

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The methylation of proteins and phospholipids has been demonstrated in mammalian sperm. The role of these methylation reactions in the regulation of sperm motility is, however, unclear. A combination of agents [adenosine, L‐homocysteine and erythro‐9‐(2‐hydroxyl‐3‐nonyl) adenine (EHNA)] known to increase the level of S‐adenosylhomocysteine (AdoHcy), a competitive inhibitor of S‐adenosylmethionine (AdoMet)‐mediated methylations, has been shown to inhibit rabbit sperm motility. The level of AdoHcy in response to these agents has, however, not been measured. Therefore, enzymatic protein carboxylmethylation (PCM) and the consequences of its inhibition by elevated intrasperm AdoHcy levels on motility were studied using bovine sperm. Incubation of bovine cauda epididymal sperm with L‐[methyl‐3H]methionine resulted in a linear increase in PCM for up to 2 h. Treatment of sperm with adenosine (0.5 mM), L‐homocysteine (0.5 mM), and EHNA (0.25 mM) produced a dramatic increase in AdoHcy levels after 15 min and a 97% inhibition of PCM after 0.5 h, followed by an inhibition of sperm motility (58% and 97%) after 1 and 2 h. Similar but less marked results were obtained with L‐homocysteine (0.5 mM) alone. Individually, cycloleucine (20 mM), an inhibitor of AdoMet synthetase, and adenosine (0.5 mM) also inhibited PCM (87% and 70%, respectively) after 2 h but had no effect on sperm motility or AdoHcy levels. These studies show for the first time that agents that elevate AdoHcy levels inhibit sperm motility. This, however, leaves open the question of whether protein carboxylmethylation or other methyl transfer reactions, eg, involving phospholipid, might be critical to motility inhibition by AdoHcy. Thus, the mechanism by which AdoHcy inhibits sperm motility remains unclear.

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Methylation of a membrane protein involved in bacterial chemotaxis.

Cited by 222 publications

References 29 publications

Sensory transduction in Escherichia coli : Role of a protein methylation reaction in sensory adaptation

Sensory transduction in Escherichia coli : Role of a protein methylation reaction in sensory adaptation

Regulation of Macrophage Lysosomal Secretion by Adenosine, Adenosine Phosphate Esters, and Related Structural Analogues of Adenosine

The involvement of methyl transfer reactions and S‐adenosylhomocysteine in the regulation of bovine sperm motility

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