Molecular evolution of protein-RNA mimicry as a mechanism for translational control.

Abstract:

:Elongation factor P (EF-P) is a conserved ribosome-binding protein that structurally mimics tRNA to enable the synthesis of peptides containing motifs that otherwise would induce translational stalling, including polyproline. In many bacteria, EF-P function requires post-translational modification with (R)-β-lysine by the lysyl-tRNA synthetase paralog PoxA. To investigate how recognition of EF-P by PoxA evolved from tRNA recognition by aminoacyl-tRNA synthetases, we compared the roles of EF-P/PoxA polar contacts with analogous interactions in a closely related tRNA/synthetase complex. PoxA was found to recognize EF-P solely via identity elements in the acceptor loop, the domain of the protein that interacts with the ribosome peptidyl transferase center and mimics the 3'-acceptor stem of tRNA. Although the EF-P acceptor loop residues required for PoxA recognition are highly conserved, their conservation was found to be independent of the phylogenetic distribution of PoxA. This suggests EF-P first evolved tRNA mimicry to optimize interactions with the ribosome, with PoxA-catalyzed aminoacylation evolving later as a secondary mechanism to further improve ribosome binding and translation control.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Katz A,Solden L,Zou SB,Navarre WW,Ibba M

doi

10.1093/nar/gkt1296

subject

Has Abstract

pub_date

2014-03-01 00:00:00

pages

3261-71

issue

5

eissn

0305-1048

issn

1362-4962

pii

gkt1296

journal_volume

42

pub_type

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