An evolutionary ratchet leading to loss of elongation factors in eukaryotes

BMC Evolutionary Biology

Vasili Hauryliuk⁴  Piotr Kamenski³  Martin Carr²  Tanel Tenson¹  Axel Soosaar¹  Ivan Chicherin³  Anton Kuzmenko³  Gemma C Atkinson⁴ 

[1] University of Tartu, Institute of Technology, Nooruse 1, 50411 Tartu, Estonia;School of Applied Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, UK;Department of Molecular Biology, Faculty of Biology, Moscow State University, Moscow, Russia;Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Umeå, Sweden

关键词: Eukaryotes;    Molecular evolution;    GEF;    GTPase;    Elongation factor;    Ribosome;    eEF1B;    EFL;    eEF1A;   

Others  :  857924
DOI  :  10.1186/1471-2148-14-35

 received in 2013-09-10, accepted in 2014-02-17,  发布年份 2014

【 摘 要 】

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.

【 授权许可】

   
2014 Atkinson et al.; licensee BioMed Central Ltd.

【 图 表 】

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