RimJ-Catalyzed Sequence-Specific Protein N-Terminal Acetylation in Escherichia coli ()
ABSTRACT
In order to establish the sequence dependence of RimJ-mediated protein N-terminal acetylation in E. coli, the Z-domain variants differing by the second or third amino acid residue were expressed and analyzed by mass spectrometry. Only subsequent to the initiating methionine residue cleavage, the RimJ-catalyzed N-terminal acetylation mainly occurred at the N-terminal serine and threonine residues and was significantly enhanced by hydrophobic or negatively charged residues in the penultimate position.
Share and Cite:
Perez, L. and Ryu, Y. (2015) RimJ-Catalyzed Sequence-Specific Protein N-Terminal Acetylation in
Escherichia coli.
Advances in Bioscience and Biotechnology,
6, 182-193. doi:
10.4236/abb.2015.63018.
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