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ProteomicsFast light changes promote distinct responses of plastid protein acetylation marks
Protein acetylation is a key recurring co- and posttranslational modification. How different types of acetylation respond to the same environmental stress is unknown. A member of the newly discovered family of plastid acetyltransferases (GNAT2), which is featuring both lysine- and N-terminal acetyl...
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress) 
2024-08-19 | PXD040517 | JPOST Repository
ProteomicsGlobal profiling of acetylation reveals a new family with dual-specific lysine and N-terminal acetyltransferase activity in the plastids of Arabidopsis
Protein acetylation is a universally conserved modification occurring on N-termini (N--acetylation, NTA) and on internal lysines residues (-lysine-acetylation, KA). So far, NTA and KA were known to be supported by distinct families of enzymes (NATs and KATs, respectively), despite most of them sha...
ORGANISM(S): Escherichia Coli 
2020-07-07 | PXD015875 | JPOST Repository
ProteomicsThe state transition acetyltransferase GNAT2 interacts with GNAT1 and GNAT3 in independent complexes
The acetylation of amino groups within proteins is one of the major posttranslational modifications (PTMs) in all organisms. N-terminal acetyltransferases (NATs) or lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from the donor substrate acetyl coenzyme A (Ac-CoA) to the t...
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress) 
2024-08-19 | PXD044167 | JPOST Repository
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