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Effect of 5'‐methylthioadenosine on in vivo methyl esterification of human erythrocyte membrane proteins
Author(s) -
Galletti Patrizia,
Oliva Adriana,
Manna Caterina,
Della Ragione Fulvio,
Cartenì-Farina Maria
Publication year - 1981
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(81)80250-5
Subject(s) - medical school , erythrocyte membrane , chemistry , biochemistry , medicine , membrane , medical education
1. Introduction The enzyme S-adenosylmethionine:protein car- boxyl-U-methyl transferase (EC 2.1 .1.24; protein methylase II) methyl esterifies the aspartyl and/or glutamyl residues of preformed proteins, using S-adenosylmethionine as the methyl donor [ 141. The protein carboxyl methyl esters formed are un- stable and undergo rapid hydrolysis at physiological pH and temperature yielding methanol [5,6]. Several membrane proteins were shown to be the endogenous substrates for the enzyme in both prokaryotic and eukaryotic cells [ 1,7--91 and a number of studies were done to determine the physiological roles of this selec- tive, post-translational, protein methylation in mem- brane functions. The high activity of PM II and the large amounts of its membrane-bound endogenous substrates in nervous and endocrine tissues suggest a role of this reaction in the synaptic function [lo] and neurosecretory processes [ 1 O-l 21. In