A Computational Study of Elongation Factor G (EFG) Duplicated Genes Diverged Nature Underlying the Innovation on the Same Structural Template 英文参考文献.docVIP
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A Computational Study of Elongation Factor G (EFG) Duplicated Genes Diverged Nature Underlying the Innovation on the Same Structural Template 英文参考文献
AComputationalStudyofElongationFactorG(EFG)
DuplicatedGenes:DivergedNatureUnderlyingthe
InnovationontheSameStructuralTemplate
To?nuMargus1,2*,MaidoRemm1,2,TanelTenson3
1DepartmentofBioinformatics,InstituteofMolecularandCellBiologyatUniversityofTartu,Tartu,Estonia,2EstonianBiocentre,Tartu,Estonia,3InstituteofTechnology
atUniversityofTartu,Tartu,Estonia
Abstract
Background:ElongationfactorG(EFG)isacoretranslationalproteinthatcatalyzestheelongationandrecyclingphasesof
translation.AmorecomplexpictureofEFG’sevolutionandfunctionthanpreviouslyacceptedisemergingfromanalyzesof
heterogeneous EFG family members. Whereas the gene duplication is postulated to be a prominent factor creating
functional novelty, the striking divergence between EFG paralogs can be interpreted in terms of innovation in gene
function.
Methodology/PrincipalFindings:WepresentacomputationalstudyoftheEFGproteinfamilytocovertheroleofgene
duplicationintheevolutionofproteinfunction.Usingphylogeneticmethods,genomecontextconservationandinsertion/
deletion(indel)analysiswedemonstratethattheEFGgenecopiesformfoursubfamilies:EFGI,spdEFG1,spdEFG2,andEFG
II. Theseancient genefamilies differ by theirindispensability, degree ofdivergence andnumberof indels. We showthe
distributionofEFGsubfamiliesanddescribeevidencesforlateralgenetransferandrecentduplications.Extendedstudiesof
the EFG II subfamily concern its diverged nature. Remarkably, EFG II appears to be a widely distributed and a much-
diversifiedsubfamilywhosesubdivisionscorrelatewithphylumorclassborders.TheEFGIIsubfamilyspecificcharacteristics
arelowconservationoftheGTPasedomain,domainsIIandIII;absenceofthetrGTPasespecificG2consensusmotif‘‘RGITI’’;
andtwelveconservedpositionscommontothewholesubfamily.TheEFGIIspecificfunctionalchangescouldberelatedto
changesinthepropertiesofnucleotidebindingandhydrolysisandstrengthenedionicinteractionsbetweenEFGIIandthe
ribosome,particularlybetweenpartsofthedecodingsiteandloopIofdomainIV.
Conclusions/Significance: Our work, for
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