TY  - JOUR
N1  - Open Access
ID  - open1895
UR  - http://www.nature.com/articles/srep28892
A1  - Pathak, Deepika
A1  - Bhat, Aadil Hussain
A1  - Sapehia, Vandana
A1  - Rai, Jagdish
A1  - Rao, Alka
Y1  - 2016///
N2  - N?-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by N?-acetyltransferases (NATs). Although present in all three domains of life, it is little understood in bacteria. The functional grouping of NATs into six types NatA - NatF, in eukaryotes is based on subunit requirements and stringent substrate specificities. Bacterial orthologs are phylogenetically divergent from eukaryotic NATs, and only a couple of them are characterized biochemically. Accordingly, not much is known about their substrate specificities. Rv3420c of Mycobacterium tuberculosis is a NAT ortholog coding for RimI(Mtb). Using in vitro peptide-based enzyme assays and mass-spectrometry methods, we provide evidence that RimI(Mtb) is a protein N?-acetyltransferase of relaxed substrate specificity mimicking substrate specificities of eukaryotic NatA, NatC and most competently that of NatE. Also, hitherto unknown acetylation of residues namely, Asp, Glu, Tyr and Leu by a bacterial NAT (RimI(Mtb)) is elucidated, in vitro. Based on in vivo acetylation status, in vitro assay results and genetic context, a plausible cellular substrate for RimI(Mtb) is proposed.
PB  - NPG
JF  - Scientific reports
VL  - 6
KW  - Mycobacterium tuberculosis; Bioinformatics
SN  - 2045-2322
TI  - Biochemical evidence for relaxed substrate specificity of N?-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis.
ER  -