作者: Shinjinee Sengupta , Paramita Chaudhuri , Sagar Lahiri , Trina Dutta , Shakri Banerjee
DOI: 10.1002/JCP.22317
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摘要: The current study was undertaken to correlate post-translational protein modification by methylation with the functionality of enzymes involved in trehalose metabolism Saccharomyces cerevisiae. Trehalose is an economically important disaccharide providing protection against various kinds stresses. It also acts as a source cellular energy storing glucose. Methyl group donor S-adenosyl L-methionine (AdoMet) and inhibitor-oxidized adenosine (AdOx) were used for study. AdoMet delayed initial growth of the cells but overall rate remained same suggesting its interference G1 phase cell cycle. Metabolic-altered enzyme activities acid trehalase (AT), neutral (NT), trehalose-6-phosphate synthase (TPS) observed when treated with AdOx separately. A positive effect TPS, hence, it purified three different conditions, using AdoMet, AdOx, control. Differences mobility methylated, methylation-inhibited, control TPS during acidic native gel electrophoresis confirmed occurrence induced methylation. Hydrolysis under alkaline pH conditions revealed that of TPS than O-methylation. MALDI-TOF analysis trypsin-digested samples and control increase 18 Da mass methylated peptides introduction methyl ester TPS. Results of amino corroborated presence cysteine. data presented here strongly suggests production was enhanced due arising from carboxymethylation cysteine residues. J. Cell. Physiol. 226: 158–164, 2010. � 2010 Wiley-Liss, Inc.