The Molecular Basis for the Post-Translational Addition of Amino Acids by L/F Transferase in the N-End Rule Pathway

Title:The Molecular Basis for the Post-Translational Addition of Amino Acids by L/F Transferase in the N-End Rule Pathway

Volume: 16 Issue: 2

Author(s): Angela Wai S. Fung and Richard P. Fahlman

Affiliation:

Keywords: aa-tRNA, Dupli-GNAT superfamily, L/F transferase, N-end rule, non-ribosomal peptide bond formation, posttranslational addition of amino acid.

Abstract: The N-end rule pathway is a conserved targeted proteolytic process observed in organisms ranging from eubacteria to mammals. The N-end rule relates the metabolic stability of a protein to its N-terminal amino acid residue. The identity of the N-terminal amino acid residue is a primary degradation signal, often referred to as an N-degron, which is recognized by the components of the N-end rule when it is a destabilizing N-terminus. N-degrons may be exposed by non-processive proteolytic cleavages or by post-translational modifications. One modification is the post-translational addition of amino acids to the N-termini of proteins, a reaction catalyzed by aminoacyl-tRNA protein transferases. The aminoacyl-tRNA protein transferase in eubacteria like Escherichia coli is L/F transferase. Recent investigations have reported unexpected observations regarding the L/F transferase catalytic mechanism and its mechanisms of substrate recognition. Additionally, recent proteome-wide identification of putative in vivo substrates facilitates hypothesis into the yet elusive biological functions of the prokaryotic N-end rule pathway. Here we summarize the recent findings on the molecular mechanisms of catalysis and substrate recognition by the E. coli L/F transferase in the prokaryotic N-end rule pathway.

Cite this article as:

S. Fung Wai Angela and Fahlman P. Richard, The Molecular Basis for the Post-Translational Addition of Amino Acids by L/F Transferase in the N-End Rule Pathway, Current Protein & Peptide Science 2015; 16 (2) . https://dx.doi.org/10.2174/1389203716666150112095726

DOI https://dx.doi.org/10.2174/1389203716666150112095726	Print ISSN 1389-2037
Publisher Name Bentham Science Publisher	Online ISSN 1875-5550