阴道毛滴虫的metacaspas样蛋白酶:计算机鉴定和表征。

IF 3.5 4区 生物学 Q2 MICROBIOLOGY
Julio César Torres-Romero, María Elizbeth Alvarez-Sánchez, Marcos Morales-Reyna, Andrea Bellavista-Caballero, Rodrigo Arreola, Leidi C Alvarez-Sánchez, Julio Lara-Riegos
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引用次数: 0

摘要

半胱天冬酶(Metacaspases, MCA)是半胱氨酸依赖性蛋白酶,与半胱天冬酶密切相关。在原生动物中,MCA在程序性细胞死亡(PCD)中起重要作用。在阴道毛滴虫中,一种类似于细胞凋亡的PCD已被描述,但这种机制的激活因子尚未得到证实。我们使用共识MCA域在阴道T.数据库中进行了全基因组的计算机分析。共检索到15个mca样序列的蛋白质注释。只有7/15的序列(TvMCA1-6和TvMCA9)被注释为假定的MCA,与用于查询的共识序列相比,显示出相似的氨基酸长度范围。通过硅分析,我们发现它们是耐热、亲水的蛋白质,分子量在27 ~ 33 KDa之间,理论等电点在5.08 ~ 8.57之间。系统发育分析表明,预测的TvMCA蛋白具有相似的保守基序。通过同源性建模的三维结构预测表明,TvMCA蛋白与结晶MCA蛋白具有相似的构象。综上所述,我们的研究结果表明,这些滴虫蛋白与MCA蛋白一样具有保守的序列,并表明它们可能在这种寄生虫的pcd样机制中负责蛋白水解活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Metacaspases-Like Proteases of Trichomonas vaginalis: In Silico Identification and Characterization.

Metacaspases (MCA), are cysteine-dependent proteases closely related to caspases. In protozoa, MCA plays an important role in programmed cell death (PCD). In Trichomonas vaginalis, a kind of PCD that resembles apoptosis has been described, but the activators of this mechanism have not been demonstrated. We performed a genome-wide in silico analysis in the T. vaginalis database using consensus MCA domains. A total of 15 protein annotations for MCA-like sequences were retrieved. Only 7/15 (TvMCA1-6 and TvMCA9) of the sequences were annotated as putative MCA and exhibited a similar range of amino acid length in comparison to the consensus sequences used for the query. By in silico analysis, we found that they are thermostable, hydrophilic proteins with molecular weights ranging from 27 to 33 KDa and their theoretical isoelectric points are in a 5.08-8.57 range. The phylogenetic analysis showed the similarity of conserved motifs for the predicted TvMCA proteins. 3D structure prediction by homology modeling demonstrated that TvMCA proteins show a similar conformation to crystallized MCA proteins. Taken together, our results indicate that these trichomonad proteins have conserved sequences like MCA proteins and suggest that they may be responsible for proteolytic activity during a PCD-like mechanism in this parasite.

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来源期刊
Journal of Basic Microbiology
Journal of Basic Microbiology 生物-微生物学
CiteScore
6.10
自引率
0.00%
发文量
134
审稿时长
1.8 months
期刊介绍: The Journal of Basic Microbiology (JBM) publishes primary research papers on both procaryotic and eucaryotic microorganisms, including bacteria, archaea, fungi, algae, protozoans, phages, viruses, viroids and prions. Papers published deal with: microbial interactions (pathogenic, mutualistic, environmental), ecology, physiology, genetics and cell biology/development, new methodologies, i.e., new imaging technologies (e.g. video-fluorescence microscopy, modern TEM applications) novel molecular biology methods (e.g. PCR-based gene targeting or cassettes for cloning of GFP constructs).
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