The N-terminal acetyltransferase NatB in Saccharomyces cerevisiae consists of the catalytic subunit Nat3p and the associated subunit Mdm20p. We here extend our present knowledge about the physiological role of NatB by a combined proteomics and phenomics approach. We found that strains deleted for either NAT3 or MDM20 displayed different growth rates and morphologies in specific stress conditions, demonstrating that the two NatB subunits have partly individual functions. Earlier reported phenotypes of the nat3Delta strain have been associated with altered functionality of actin cables. However, we found that point mutants of tropomyosin that suppress the actin cable defect observed in nat3Delta only partially restores wild-type growth and morphology, indicating the existence of functionally important acetylations unrelated to actin cable function. Predicted NatB substrates were dramatically overrepresented in a distinct set of biological processes, mainly related to DNA processing and cell cycle

N-terminal acetyltransferase (Nats) complex is responsible for protein N-terminal acetylation (Nα-acetylation), which is one of the most common covalent modifications of eukaryotic proteins. Although genome-wide investigation and characterization of Nat catalytic subunits (CS) and auxiliary subunits (AS) have been conducted in yeast and humans they remain unexplored in plants. Here we report on the identification of eleven genes encoding eleven putative Nat CS polypeptides, and five genes encoding five putative Nat AS polypeptides in Populus. We document that the expansion of Nat CS genes occurs as duplicated blocks distributed across 10 of the 19 poplar chromosomes, likely only as a result of segmental duplication events. Based on phylogenetic analysis, poplar Nat CS were assigned to six subgroups, which corresponded well to the Nat CS types (CS of Nat A-F), being consistent with previous reports in humans and yeast. In silico analysis of microarray data showed that in the process of normal

An N-terminal acetyltransferase subtype that consists of the Naa50p Catalytic Subunit, and the Naa10p and Naa15p auxiliary subunits. It has specificity for the N-terminal Methionine of Peptides where the next amino acid in the chain is hydrophobic ...

Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate.

N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:25886145). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides (PubMed:25886145). Non-essential component of the NatA N-terminal acetyltransferase (PubMed:14517307).

To address the mechanism behind the altered cytoskeleton organization phenotypes of NAA80-KO cells, we analyzed the recovery rates of cytoskeletal structures in cells treated with the actin-depolymerizing drug latrunculin A (LatA). Within 60 min of LatA treatment the actin appeared to be fully depolymerized in control and NAA80-KO cells, and washout of the drug resulted in the recovery of actin filament structures, but the time of recovery was significantly delayed for NAA80-KO cells compared with control cells (Fig. S6), consistent with a direct role of actin Nt-acetylation in actin polymerization.. We next explored the in vitro effect of actin Nt-acetylation on the polymerization/depolymerization properties of actin alone or in the presence of some of the most common actin-assembly factors in cells. Cytoplasmic actin (a mixture of β and γ isoforms) was purified from control and NAA80-KO cells, and the presence or absence of Nt-acetylation was verified by Western blotting (Fig. 4A) (22). The ...

An N-terminal acetyltransferase subtype that consists of the Naa10p Catalytic Subunit and the Naa15p auxiliary subunit. The structure of this enzyme is conserved between lower and higher Eukaryotes. It has specificity for N-terminal Serine; Alanine; Threonine; Glycine; Valine; and Cystine residues and acts on nascent peptide chains after the removal of the initiator Methionine by Methionyl Aminopeptidases ...

Dr. Richard Moerschell received a Ph.D. in Biophysics from the University of Rochester in Rochester, NY. During the course of his studies he developed the technique for transforming yeast directly with synthetic oligonucleotides. In his studies, he has determined the specificity of methionine aminopeptidase and co-discovered the first N-terminal acetyltransferase. He went on to post-doctoral positions at Osaka University and Harvard Medical School where he studied ATP dependent proteases and chaperones. He has over 15 years experience in the life science industry in roles marketing and R&D. Dr. Moerschell is registered to practice as a patent agent with the US Patent Office. www.molecularpurity.com. ...

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