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Protein N-terminal acetylation
Protein N-terminal acetylation is among the most common types of protein modifications occurring on approximately 50 % of all soluble yeast proteins and more than 80 % of all soluble human proteins. Surprisingly, there is yet no clear functional understanding of how N-terminal acetylation affects proteins in general.
NatA and cancer
The human NatA complex, composed of the catalytic subunit hNaa10p (hARD1) and the auxiliary subunit hNaa15p (NATH), is the major N-terminal acetyltransferase in humans cotranslationally acetylating nascent polypeptides with Ala-, Ser-, Thr-, Val- or Gly- N-termini after cleavage of the initiator Met.
An increasing interest to the hNatA complex results from recent findings demonstrating correlation between expression of the hNatA subunits and tumour development.
Protein N-terminal acetylation - From molecular mechanisms to human disease
Almost every single eukaryotic protein is modified and such modifications are often crucial for the protein’s ability to carry out a specific function. Since proteins are involved in virtually every cellular process, many protein modifications and the enzymes catalyzing such modifications are essential for life. Furthermore, dysregulation of protein modifying enzymes are often associated with disease states. N-terminal acetylation is among the most common modifications in eukaryotes. It is catalyzed by N-terminal acetyltransferases (NATs) which are linked to cancer, genetic syndromes, and regulation of human metabolism.
(Illustration: Arnt Raae & Svein Støve, MBI)
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News
- MBI TiBS paper Editor's choice (03.04.2013)
- Book on protein acetylation (19.02.2013)
- New protein tricks from an old enzyme (02.01.2013)