Dataset Information

Nt-propionylation in yeast - Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo

ABSTRACT: a yNatA N-terminal proteome (WT) was differentialy compared with either a yNatA delta or a yNatA delta/hNatA expressing N-terminal proteome

INSTRUMENT(S): LTQ-Orbitrap

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Petra Van Damme

LAB HEAD: Petra Van Damme

PROVIDER: PRD000673 | Pride | 2013-02-27

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	PRIDE_Exp_Complete_Ac_22438.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_22438.xml.gz	Xml

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Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo.

Foyn Håvard H Van Damme Petra P Støve Svein I SI Glomnes Nina N Evjenth Rune R Gevaert Kris K Arnesen Thomas T

Molecular & cellular proteomics : MCP 20121004 1

N-terminal acetylation (Nt-acetylation) is a highly abundant protein modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), which transfer an acetyl group from acetyl coenzyme A to the alpha amino group of a nascent polypeptide. Nt-acetylation has emerged as an important protein modifier, steering protein degradation, protein complex formation and protein localization. Very recently, it was reported that some human proteins could carry a propionyl group at their N-terminus ...[more]

PMID: 23043182

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Project description:Acetylation of small molecules is widespread in nature, and in some cases, cells use this process to detoxify harmful chemicals. Streptomyces species utilize a Gcn5 N-acetyltransferase (GNAT), known as Bar, to acetylate and detoxify a self-produced toxin, phosphinothricin (PPT), a glutamate analogue. Bar homologues, such as MddA from Salmonella enterica, acetylate methionine analogues such as methionine sulfoximine (MSX) and methionine sulfone (MSO), but not PPT, even though Bar homologues are annotated as PPT acetyltransferases. S. enterica was used as a heterologous host to determine whether or not putative PPT acetyltransferases from various sources could acetylate PPT, MSX, and MSO. In vitro and in vivo analyses identified substrates acetylated by putative PPT acetyltransferases from Deinococcus radiodurans (DR_1057 and DR_1182) and Geobacillus kaustophilus (GK0593 and GK2920). In vivo, synthesis of DR_1182, GK0593, and GK2920 blocked the inhibitory effects of PPT, MSX, and MSO. In contrast, DR_1057 did not detoxify any of the above substrates. Results of in vitro studies were consistent with the in vivo results. In addition, phylogenetic analyses were used to predict the functionality of annotated PPT acetyltransferases in Burkholderia xenovorans, Bacillus subtilis, Staphylococcus aureus, Acinetobacter baylyi, and Escherichia coli IMPORTANCE: The work reported here provides an example of the use of a heterologous system for the identification of enzyme function. Many members of this superfamily of proteins do not have a known function, or it has been annotated solely on the basis of sequence homology to previously characterized enzymes. The critical role of Gcn5 N-acetyltransferases (GNATs) in the modulation of central metabolic processes, and in controlling metabolic stress, necessitates approaches that can reveal their physiological role. The combination of in vivo, in vitro, and bioinformatics approaches reported here identified GNATs that can acetylate and detoxify phosphinothricin.