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首页> 外文期刊>Proteomics >CFP10 discriminates between nonacetylated and acetylated ESAT-6 of Mycobacterium tuberculosis by differential interaction
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CFP10 discriminates between nonacetylated and acetylated ESAT-6 of Mycobacterium tuberculosis by differential interaction

机译：CFP10通过差异相互作用区分结核分枝杆菌的非乙酰化和乙酰化ESAT-6

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摘要

ESAT-6 (the 6 kDa early secreted antigenic target) protein species in short-term culture filtrate of Mycobacterium tuberculosis were separated in a 4-5 narrow range p/ gradient two-dimensional gel electrophoresis (2-DE). Eight ESAT-6 protein species were analyzed in detail by peptide mass fingerprinting matrix-assisted laser desorption/ionization-mass spectrometry as well as by electrospray ionization-tandem mass spectrometry. An N-terminal Thr acetylation was identified in four species and a C-terminal truncation was identified in two species. In 2-DE blot overlay assays, the recombinant 10 kDa culture filtrate protein (CFP10) discriminated N-terminal acetylated and nonacetylated ESAT-6 by differential interaction, whereas removal of the C-terminal 11 residues of ESAT-6 had no effects thereon. This example shows that the access to the protein species level can be a prerequisite to understand regulation of protein-protein interaction.
机译：在4-5窄范围p /梯度二维凝胶电泳（2-DE）中分离结核分枝杆菌短期培养滤液中的ESAT-6（6 kDa早期分泌的抗原靶标）蛋白种类。通过肽质谱指纹图谱辅助激光解吸/电离质谱和电喷雾电离串联质谱分析了8种ESAT-6蛋白。在四个物种中鉴定出N端Thr乙酰化，在两个物种中鉴定出C端截短。在2-DE印迹重叠分析中，重组10 kDa培养滤液蛋白（CFP10）通过差异相互作用区分了N末端的乙酰化ESAT-6和非乙酰化的ESAT-6，而去除ESAT-6的C末端11个残基对其没有影响。这个例子表明，达到蛋白质种类水平可能是理解蛋白质相互作用的先决条件。

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