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1Identifcation of the Phosphorylated Residues in TveIF5A by Mass Spectrometry显示文摘The initiation factor eIF5A in Trichomonas vaginalis(TveIF5A)is previously shown to undergo hypusination,phosphorylation and glycosylation.Three different pI isoforms of TveIF5A have been reported.The most acidic isoform(pI 5.2)corresponds to the precursor TveIF5A,whereas the mature TveIF5A appears to be the most basic isoform(pI 5.5).In addition,the intermediary isoform(pI 5.3)is found only under polyamine-depleted conditions and restored with exogenous putrescine.We propose that differences in PI are due to phosphorylation of the TveIF5A isoforms.Here,we have identifed phosphorylation sites using mass spectrometry.The mature TveIF5A contains four phosphorylated residues(S3,T55,T78 and T82).Phosphorylation at S3and T82 is also identifed in the intermediary TveIF5A,while no phosphorylated residues are found in the precursor TveIF5A.It has been demonstrated that eIF5A proteins from plants and yeast are phosphorylated by a casein kinase 2(CK2).Interestingly,a gene encoding a protein highly similar to CK2(TvCK2)is found in T.vaginalis,which might be involved in the phosphorylation of TveIF5A in T.vaginalis.Laura Itzel Quintas-Granados César López-Camarillo Jesús Fandi?o Armas Guillermo Mendoza Hernandez María Elizbeth Alvarez-Snchez 2013Genomics, Proteomics & Bioinformatics2013,11,6:0
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