Protein L-isoaspartyl methyltransferase regulates p53 activity

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Protein L-isoaspartyl methyltransferase regulates p53 activity

Protein methylation plays important roles in most, if not all, cellular processes. Lysine and arginine methyltransferases are known to regulate the function of histones and non-histone proteins through the methylation of specific sites. However, the role of the carboxyl-methyltransferase protein L-isoaspartyl methyltransferase (PIMT) in the regulation of protein functions is relatively less und...

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Distribution of an L-isoaspartyl protein methyltransferase in eubacteria.

A protein carboxyl methyltransferase (EC 2.1.1.77) that recognizes age-damaged proteins for potential repair or degradation reactions has been found in all vertebrate tissues and cells examined to date. This enzyme catalyzes the transfer of methyl groups from S-adenosylmethionine to the carboxyl groups of D-aspartyl or L-isoaspartyl residues that are formed spontaneously from normal L-aspartyl ...

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Crystal structure of human L-isoaspartyl methyltransferase.

The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged proteins by recognizing and methylating isomerized and racemized aspartyl residues in aging proteins. The crystal structure of the human enzyme containing a bound S-adenosyl-l-homocysteine cofactor is reported here at a resolution of 2.1 A. A comparison of the human enzyme to homologs from two other species reveals sever...

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Priming and accelerated ageing affect L-isoaspartyl methyltransferase activity in tomato (Lycopersicon esculentum Mill.) seed

Damage and degradation of cellular proteins is observed during age-induced seed deterioration, LIsoaspartyl protein methyltransferase (EC 2.1.1.77) is an enzyme hypothesized to play a role in limiting and repairing age-induced damage to proteins. Tomato {Lycopersicon esculentum Mill. 'New Yorker') seeds were assayed for changes in L-isoaspartyl methyltransferase activity during accelerated agei...

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The Interplay between Protein L-Isoaspartyl Methyltransferase Activity and Insulin-Like Signaling to Extend Lifespan in Caenorhabditis elegans

The protein L-isoaspartyl-O-methyltransferase functions to initiate the repair of isomerized aspartyl and asparaginyl residues that spontaneously accumulate with age in a variety of organisms. Caenorhabditis elegans nematodes lacking the pcm-1 gene encoding this enzyme display a normal lifespan and phenotype under standard laboratory growth conditions. However, significant defects in developmen...

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ژورنال

عنوان ژورنال: Nature Communications

سال: 2012

ISSN: 2041-1723

DOI: 10.1038/ncomms1933