Proteomic analysis of the Trypanosoma cruzi ribosomal proteins

被引:18
作者
Juri Ayub, Maximiliano [1 ,2 ]
Atwood, James [3 ]
Nuccio, Arthur [3 ]
Tarleton, Rick [4 ,5 ]
Levin, Mariano J. [1 ]
机构
[1] Consejo Nacl Invest Cient & Tecn, Inst Invest Ingn Genet & Biol Mol INGEBI, LaBMECH, Buenos Aires, DF, Argentina
[2] Univ Nacl San Luis, Mol Biol Lab, Catedra Ingn Genet, RA-5700 San Luis, Argentina
[3] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA
[4] Univ Georgia, Ctr Trop & Emerging Global Dis, Athens, GA 30602 USA
[5] Univ Georgia, Dept Cellular Biol, Athens, GA 30602 USA
关键词
Trypanosoma cruzi; Protein synthesis; Mass spectrometry; Ribosome; SPLICED LEADER; MESSENGER-RNA; LEISHMANIA-TARENTOLAE; MASS-SPECTROMETRY; IDENTIFICATION; CAP-4; TRICHOSANTHIN; INACTIVATION; COMPLEXES; CONTAINS;
D O I
10.1016/j.bbrc.2009.02.095
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Trypanosoma cruzi is a parasite responsible for Chagas disease. The identification of new targets for chemotherapy is a major challenge for the control of this disease. Several lines of evidences suggest that the translational system in trypanosomatids show important differences compared to other eukaryotes. However, there little is known information about this. We have performed a detailed data mining search for ribosomal protein genes in T. cruzi genome data base combined with mass spectrometry analysis of purified T cruzi ribosomes. Our results show that T cruzi ribosomal proteins have similar to 50% sequence identity to yeast ones. Nevertheless, some parasite proteins are longer due to the presence of several N- or C-terminal extensions, which are exclusive of trypanosomatids. In particular, L19 and S21 show C-terminal extensions of 168 and 164 amino acids, respectively. In addition, we detected two 60S subunit proteins that had not been previously detected in the T cruzi total proteome: namely, L22 and L42. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:30 / 34
页数:5
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