Amino acid sequence repertoire of the bacterial proteome and the occurrence of untranslatable sequences

Sharon Penias Navon, Guy Kornberg, Jin Chen, Tali Schwartzman, Albert Tsai, Elisabetta Viani Puglisi, Joseph D. Puglisi, Noam Adir

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Bioinformatic analysis of Escherichia coli proteomes revealed that all possible amino acid triplet sequences occur at their expected frequencies, with four exceptions. Two of the four underrepresented sequences (URSs) were shown to interfere with translation in vivo and in vitro. Enlarging the URS by a single amino acid resulted in increased translational inhibition. Single-molecule methods revealed stalling of translation at the entrance of the peptide exit tunnel of the ribosome, adjacent to ribosomal nucleotides A2062 and U2585. Interaction with these same ribosomal residues is involved in regulation of translation by longer, naturally occurring protein sequences. The E. coli exit tunnel has evidently evolved to minimize interaction with the exit tunnel and maximize the sequence diversity of the proteome, although allowing some interactions for regulatory purposes. Bioinformatic analysis of the human proteome revealed no underrepresented triplet sequences, possibly reflecting an absence of regulation by interaction with the exit tunnel.

Original languageEnglish (US)
Pages (from-to)7166-7170
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume113
Issue number26
DOIs
StatePublished - Jun 28 2016
Externally publishedYes

Keywords

  • Bioinformatics
  • Single-molecule methods
  • Stalling peptides
  • Translation
  • Underrepresented sequences

ASJC Scopus subject areas

  • General

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