Abstract
It is increasingly evident that several covalent post-translational modifications of proteins play important regulatory roles in many cellular functions (Uy and Wold, 1977; Paik and Kim, 1980). These reactions occur on preformed proteins by group transfer reactions on specific amino acid side chains and thus have the capacity to modulate protein function post-synthetically. Among these modifications, carboxyl methylations of proteins are being studied in membranes of prokaryotes and eukaryotes in relation to their effects on membrane functions: Thus, the role of membrane methylation in motile bacteria has now been established as the biochemical sensory input signal in chemotactic action (Springer et al., 1979; Springer and Koshland, 1977). In the case of eukaryotes, methylation is studied in various membrane systems involving secretion/excitation and motility/chemotaxis (Diliberto et al., 1976b; Gagnon et al., 1979; O’Dea et al., 1978).
This investigation was supported by General Medical Sciences Research Grant GM20594 and Biomedical Research Support Grant S07 RR05417 from the Division of Research Resources, National Institutes of Health. * To whom correspondence should be addressed.
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Kim, S., Ro, JY., Manna, C., Glushko, V.G. (1982). Enzymatic carboxyl methyl esterification of proteins: Studies on sickle erythrocyte membrane . In: Biochemistry of S-Adenosylmethionine and Related Compounds. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06343-7_5
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