Abstract
The protein acetylation of either the α-amino groups of amino-terminal residues or of internal lysine or cysteine residues is one of the major posttranslational protein modifications that occur in the cell with repercussions at the protein as well as at the metabolome level. The lysine acetylation status is determined by the opposing activities of lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), which add and remove acetyl groups from proteins, respectively. A special group of KDACs, named sirtuins, that require NAD+ as a substrate have received particular attention in recent years. They play critical roles in metabolism, and their abnormal activity has been implicated in several diseases. Conversely, the modulation of their activity has been associated with protection from age-related cardiovascular and metabolic diseases and with increased longevity. The benefits of either activating or inhibiting these enzymes have turned sirtuins into attractive therapeutic targets, and considerable effort has been directed toward developing specific sirtuin modulators. This review summarizes the protein acylation/deacylation processes with a special focus on the current developments in the sirtuin research field.
Highlights
Proteins are the structural and functional base of all living organisms
Sirt6 and Sirt7 bind to certain transcription factors, which recruit them to different chromatin regions, where they catalyze the deacetylation of a specific histone at specific target genes [118,119,120]
Several studies suggest that caloric restriction increases the expression levels of sirtuins, with the exception of Sirt4 [131,132,133] This relation between sirtuin activation and increased lifespan has suggested that sirtuins may have a role in the beneficial effects elicited by a caloric restriction diet [134]
Summary
Proteins are the structural and functional base of all living organisms. To date, the number of proteins that comprise the human proteome is still elusive. The analysis of the human genome shows the existence of approximately 25,000 protein-coding genes [1]. To date, more than 90,000 different human proteins have been identified This discrepancy has been attributed to three district mechanisms: the alternative splicing of precursor mRNAs, single amino acid polymorphisms (SAPs) and posttranslational modifications (PTMs) [2,3,4]. Together, these modifications raise the complexity of the proteomes by two to three orders of magnitude and help to explain the discrepancy between the complexity of vertebrate organisms and the sizes of their encoded genomes [2,5]. Sci. 2020, 21, 8609 bound methionine aminopeptidases, and the acetyl group is added to the residue that is positioned immediately after the excised methionine
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