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Hirel, P.H., Schmitter, J.M., Dessen, P., Fayat, G. and Blanquet, S. (1989) Extent of N-Terminal Methionine Excision from Escherichia coli Proteins Is Governed by the Side-Chain Length of the Penultimate Amino-Acid. Proceedings of the National Academy of Sciences of the United States of America, 86, 8247-8251.
http://dx.doi.org/10.1073/pnas.86.21.8247

has been cited by the following article:

• TITLE: RimJ-Catalyzed Sequence-Specific Protein N-Terminal Acetylation in Escherichia coli

  AUTHORS: Lina F. Bernal- Perez, Youngha Ryu

  KEYWORDS: Protein N-Terminal Processing, Protein N-Terminal Acetylation, RimJ

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.6 No.3, March 26, 2015

  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.