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Identifcation of the Phosphorylated Residues in TveIF5A by Mass Spectrometry

Identifcation of the Phosphorylated Residues in TveIF5A by Mass Spectrometry

作     者:Laura Itzel Quintas-Granados César López-Camarillo Jesús Fandi?o Armas Guillermo Mendoza Hernandez María Elizbeth Alvarez-Snchez 

作者机构:Genomic Sciences PostgraduateAutonomous University of Mexico City (UACM) Department of BiochemistryFaculty of MedicineNational Autonomous University of Mexico 

出 版 物:《Genomics, Proteomics & Bioinformatics》 (基因组蛋白质组与生物信息学报(英文版))

年 卷 期:2013年第11卷第6期

页      面:378-384页

核心收录:

学科分类:0710[理学-生物学] 07[理学] 08[工学] 09[农学] 071007[理学-遗传学] 0901[农学-作物学] 0836[工学-生物工程] 090102[农学-作物遗传育种] 

基  金:supported by grants from Consejo Nacional de Ciencia y Tecnolog'a(CONACyT Grant No.83808)Mexico awarded to MEAS Instituto de Ciencia y Tecnolog'a del Distrito Federal(ICyTDF Grant No.221/2011,328/2011,18/2011 and 321/2009) 

主  题:Trichomonas vaginalis Initiation factor eIF5A Phosphoryiation Casein kinase 2 

摘      要:The initiation factor elF5A in Trichomonas vaginalis (TvelF5A) is previously shown to undergo hypusination, phosphorylation and glycosylation. Three different pI isoforms of TvelF5A have been reported. The most acidic isoform (pI 5.2) corresponds to the precursor TvelF5A, whereas the mature TvelF5A 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 TvelF5A isoforms. Here, we have identified phosphorylation sites using mass spectrometry. The mature TvelF5A contains four phosphorylated residues ($3, T55, T78 and T82). Phosphorylation at $3 and T82 is also identified in the intermediary TvelF5A, while no phosphorylated residues are found in the precursor TvelF5A. It has been demonstrated that elF5A 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 TvelF5A in T. vaginalis.

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