嗜热嗜酸Euryarchaeon Picrophilus torridus的蛋白质组学和胞质蛋白质组学计算分析

IF 0.5 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS
N. Singhal, Anjali Garg, Nirpendra Singh, Manish Kumar, M. Goel
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引用次数: 0

摘要

torridus是一种嗜热酸性古菌,在极低的pH值(0-1)和高温(50-60°C)下繁殖。因此,它是一种适合研究微生物遗传学和代谢适应极端酸性和中等热环境的生物。本研究采用无凝胶液相色谱质谱法(LC-MS/MS)对墨西哥纸虫的细胞质蛋白质组进行了分析。采用无凝胶液相色谱-质谱联用技术,提取并鉴定了torridus的胞质蛋白。通过基因本体通路分析和蛋白-蛋白相互作用研究,了解各种胞质蛋白在维持嗜热酸性环境中的作用。此外,还进行了假设/未表征蛋白的结构域分析。采用无凝胶LC-MS/MS技术,共鉴定出408种torridus胞质蛋白,其中36种为假设或未鉴定的蛋白。因此,我们可以鉴定出26.58%的torridus理论蛋白质组。大多数细胞质蛋白被观察到是多功能的,并参与与微生物代谢有关的活动。与之前采用凝胶- LC-MS方法鉴定番茄假单胞菌胞质蛋白的研究结果相比,无凝胶- LC-MS方法鉴定的蛋白数量更多,分子量更高或更低。本研究可为进一步研究其他嗜热酸古菌的蛋白质组学提供有益的基础,并为进一步研究其他嗜热酸古菌的蛋白质组学奠定基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Proteomics and Computational Analysis of Cytosolic Proteome of a Thermoacidophilic Euryarchaeon Picrophilus torridus
Picrophilus torridus is a thermoacidophilic archaeon which thrives in an extremely low pH (0-1) and high temperatures (50-60°C). Thus, it is a suitable organism to study microbial genetics and metabolic adaptations to extreme acidic and moderate thermal environment. In the present study we have conducted a global proteome analysis of P. torridus and discerned the cytosolic proteome of P. torridus using gel-free, liquid chromatography mass spectrometry (LC-MS/MS). The cytosolic proteins of P. torridus were extracted and identified using gel-free, LC-MS/MS. Gene Ontology based pathway analysis and protein-protein interaction studies were performed to understand the role of various cytosolic proteins in sustaining the thermoacidophilic environment. Also, domain analysis of hypothetical/uncharacterized proteins was performed. Using gel-free LC-MS/MS, 408 cytosolic proteins of P. torridus were identified, including 36 hypothetical/uncharacterized proteins. Thus, we could identify 26.58 % of the theoretical proteome of P. torridus. Majority of the cytosolic proteins were observed to be multi-functional and involved in activities related to microbial metabolism. Comparison with an earlier study which used gel-based LC-MS analysis to identify cytosolic proteins of P. torridus revealed that gel-free LC-MS was better in identifying more number of proteins and also, higher/lower molecular weight proteins. The information discerned in this study might add to the knowledge-base of P. torridus proteome and provide a useful basis for further proteomic studies on other thermoacidophilic archaea.
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来源期刊
Current Proteomics
Current Proteomics BIOCHEMICAL RESEARCH METHODS-BIOCHEMISTRY & MOLECULAR BIOLOGY
CiteScore
1.60
自引率
0.00%
发文量
25
审稿时长
>0 weeks
期刊介绍: Research in the emerging field of proteomics is growing at an extremely rapid rate. The principal aim of Current Proteomics is to publish well-timed in-depth/mini review articles in this fast-expanding area on topics relevant and significant to the development of proteomics. Current Proteomics is an essential journal for everyone involved in proteomics and related fields in both academia and industry. Current Proteomics publishes in-depth/mini review articles in all aspects of the fast-expanding field of proteomics. All areas of proteomics are covered together with the methodology, software, databases, technological advances and applications of proteomics, including functional proteomics. Diverse technologies covered include but are not limited to: Protein separation and characterization techniques 2-D gel electrophoresis and image analysis Techniques for protein expression profiling including mass spectrometry-based methods and algorithms for correlative database searching Determination of co-translational and post- translational modification of proteins Protein/peptide microarrays Biomolecular interaction analysis Analysis of protein complexes Yeast two-hybrid projects Protein-protein interaction (protein interactome) pathways and cell signaling networks Systems biology Proteome informatics (bioinformatics) Knowledge integration and management tools High-throughput protein structural studies (using mass spectrometry, nuclear magnetic resonance and X-ray crystallography) High-throughput computational methods for protein 3-D structure as well as function determination Robotics, nanotechnology, and microfluidics.
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