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A Comprehensive Analysis of Lysine Acetylation in Ribosomal Proteins
Author(s) -
Koc Hasan,
Cimen Huseyin,
Stallard Adam,
Koc Zeynep C,
Koc Emine C
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.958.2
Subject(s) - ribosome , ribosomal protein , mitochondrial ribosome , acetylation , ribosomal rna , lysine , translation (biology) , biochemistry , biology , transfer rna , protein superfamily , protein biosynthesis , conserved sequence , eukaryotic ribosome , chemistry , microbiology and biotechnology , messenger rna , peptide sequence , amino acid , gene , rna
Protein synthesis is one of the most conserved processes in living organisms; specifically, the conservation between mammalian mitochondrial and bacterial translation machineries/ribosomes has been the most surprising one of all. Our comprehensive studies of post‐translational modifications (PTMs) to ribosomal proteins and large‐scale mass spectrometry (MS)‐based PTM mapping studies from several other laboratories suggest that the mitochondrial and bacterial ribosomes are highly modified by acetylation at their ε‐amino groups of Lys residues. The majority of the modified proteins were found to be located in the essential regions of ribosome function including, mRNA‐ and tRNA‐binding path, peptide exit tunnel, and the L1 and L7/L12 stalks. Interestingly, not only the proteins with conserved homologous functions but also the conserved residues are post‐translationally modified in both systems. The nature of this modification in both mitochondrial and bacterial ribosomes indicates that it is an essential and evolutionarily conserved mechanism for the regulation of protein synthesis. Supported by NIH grant R01GM071034 (E.C.K.).