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An evolutionary ratchet leading to loss of elongation factors in eukaryotes

Atkinson, Gemma C. LU orcid ; Kuzmenko, Anton ; Chicherin, Ivan ; Soosaar, Axel ; Tenson, Tanel ; Carr, Martin ; Kamenski, Piotr and Hauryliuk, Vasili LU orcid (2014) In BMC Evolutionary Biology 14. p.1-9
Abstract

Background: The GTPase eEF1A is the eukaryotic factor responsible for the essential, universal function of aminoacyl-tRNA delivery to the ribosome. Surprisingly, eEF1A is not universally present in eukaryotes, being replaced by the paralog EFL independently in multiple lineages. The driving force behind this unusually frequent replacement is poorly understood. Results: Through sequence searching of genomic and EST databases, we find a striking association of eEF1A replacement by EFL and loss of eEF1A's guanine exchange factor, eEF1Bα, suggesting that EFL is able to spontaneously recharge with GTP. Sequence conservation and homology modeling analyses indicate several sequence regions that may be responsible for EFL's lack of requirement... (More)

Background: The GTPase eEF1A is the eukaryotic factor responsible for the essential, universal function of aminoacyl-tRNA delivery to the ribosome. Surprisingly, eEF1A is not universally present in eukaryotes, being replaced by the paralog EFL independently in multiple lineages. The driving force behind this unusually frequent replacement is poorly understood. Results: Through sequence searching of genomic and EST databases, we find a striking association of eEF1A replacement by EFL and loss of eEF1A's guanine exchange factor, eEF1Bα, suggesting that EFL is able to spontaneously recharge with GTP. Sequence conservation and homology modeling analyses indicate several sequence regions that may be responsible for EFL's lack of requirement for eEF1Bα. Conclusions: We propose that the unusual pattern of eEF1A, eEF1Bα and EFL presence and absence can be explained by a ratchet-like process: if either eEF1A or eEF1Bα diverges beyond functionality in the presence of EFL, the system is unable to return to the ancestral, eEF1A:eEFBα-driven state.

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author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
keywords
eEF1A, eEF1B, EFL, Elongation factor, Eukaryotes, GEF, GTPase, Molecular evolution, Ribosome
in
BMC Evolutionary Biology
volume
14
article number
35
pages
1 - 9
publisher
BioMed Central (BMC)
external identifiers
  • pmid:24564225
  • scopus:84896720151
ISSN
1471-2148
DOI
10.1186/1471-2148-14-35
language
English
LU publication?
yes
additional info
Funding Information: We thank Barry Leadbeater for providing M. brevicollis culture, Terry Kinzy for providing S. cerevisiae strains TKY961 and JWY4231 as well as plasmid pJWB2937, and Thomas D Fox for the S. cerevisiae DUL2 strain and experimental advice. This work was supported by the funds from European Regional Development Fund through the Centre of Excellence in Chemical Biology (VH and TT), Estonian Science Foundation grants (ETF9012 and PUT37 to VH, ETF9020 to GCA); Swedish Research council and Umeå University (VH); Archimedes Foundation (AK); “U.M.N.I. K” program (AK), Russian Foundation for Basic Research (AK, IC and PK) and European Social Fund grant “Mobilitas” MJD99 (GCA). Copyright: Copyright 2014 Elsevier B.V., All rights reserved.
id
2d788155-4cf0-4e2b-970d-0bee59caa7e5
date added to LUP
2021-09-24 20:45:48
date last changed
2025-01-13 14:33:12
@article{2d788155-4cf0-4e2b-970d-0bee59caa7e5,
  abstract     = {{<p>Background: The GTPase eEF1A is the eukaryotic factor responsible for the essential, universal function of aminoacyl-tRNA delivery to the ribosome. Surprisingly, eEF1A is not universally present in eukaryotes, being replaced by the paralog EFL independently in multiple lineages. The driving force behind this unusually frequent replacement is poorly understood. Results: Through sequence searching of genomic and EST databases, we find a striking association of eEF1A replacement by EFL and loss of eEF1A's guanine exchange factor, eEF1Bα, suggesting that EFL is able to spontaneously recharge with GTP. Sequence conservation and homology modeling analyses indicate several sequence regions that may be responsible for EFL's lack of requirement for eEF1Bα. Conclusions: We propose that the unusual pattern of eEF1A, eEF1Bα and EFL presence and absence can be explained by a ratchet-like process: if either eEF1A or eEF1Bα diverges beyond functionality in the presence of EFL, the system is unable to return to the ancestral, eEF1A:eEFBα-driven state.</p>}},
  author       = {{Atkinson, Gemma C. and Kuzmenko, Anton and Chicherin, Ivan and Soosaar, Axel and Tenson, Tanel and Carr, Martin and Kamenski, Piotr and Hauryliuk, Vasili}},
  issn         = {{1471-2148}},
  keywords     = {{eEF1A; eEF1B; EFL; Elongation factor; Eukaryotes; GEF; GTPase; Molecular evolution; Ribosome}},
  language     = {{eng}},
  pages        = {{1--9}},
  publisher    = {{BioMed Central (BMC)}},
  series       = {{BMC Evolutionary Biology}},
  title        = {{An evolutionary ratchet leading to loss of elongation factors in eukaryotes}},
  url          = {{http://dx.doi.org/10.1186/1471-2148-14-35}},
  doi          = {{10.1186/1471-2148-14-35}},
  volume       = {{14}},
  year         = {{2014}},
}