Article
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
Cell reports - 23 Oct 2014
Starosta Agata L, Lassak Jürgen, Peil Lauri, Atkinson Gemma C, Woolstenhulme Christopher J, Virumäe Kai, Buskirk Allen, Tenson Tanel, Remme Jaanus, Jung Kirsten, Wilson Daniel N
Abstract excerpt
Bacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P) to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF-P rather than selecting against the occurrence of polyproline stretches in proteins. We have discovered that only a single polyproline stretch is invariant across all domains of life, namely a proline triplet in ValS, the tRNA...
Topics
- Amino Acid Sequence
- Conserved Sequence
- Escherichia coli
- Escherichia coli Proteins
- Evolution, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Elongation Factors
- Peptides
- Valine-tRNA Ligase