Proteomics and Computational Analysis of Cytosolic Proteome of a Thermoacidophilic Euryarchaeon Picrophilus torridus

IF 0.5 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS Current Proteomics Pub Date : 2022-04-29 DOI:10.2174/1570164619666220429121247
N. Singhal, Anjali Garg, Nirpendra Singh, Manish Kumar, M. Goel
{"title":"Proteomics and Computational Analysis of Cytosolic Proteome of a Thermoacidophilic Euryarchaeon Picrophilus torridus","authors":"N. Singhal, Anjali Garg, Nirpendra Singh, Manish Kumar, M. Goel","doi":"10.2174/1570164619666220429121247","DOIUrl":null,"url":null,"abstract":"\n\nPicrophilus 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.\n\n\n\nIn 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).\n\n\n\nThe 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.\n\n\n\nUsing 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.\n\n\n\nComparison 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.\n","PeriodicalId":50601,"journal":{"name":"Current Proteomics","volume":"95 1","pages":""},"PeriodicalIF":0.5000,"publicationDate":"2022-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Proteomics","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2174/1570164619666220429121247","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
引用次数: 0

Abstract

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.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
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
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。
求助全文
约1分钟内获得全文 去求助
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.
期刊最新文献
Exploring Phytochemical Compounds: A Computational Study for HIV-1 Reverse Transcriptase Inhibition Molecular Docking, Pharmacophore Mapping, and Virtual Screening of Novel Glucokinase Activators as Antidiabetic Agents Comprehensive Analysis of Tertiary Lymphoid Structures in Pancreatic Cancer: Molecular Characteristics and Prognostic Implications miR-124 in Neuroblastoma: Mechanistic Insights, Biomarker Potential, and Therapeutic Prospects The Relationship of Transposable Elements with Non-Coding RNAs in the Emergence of Human Proteins and Peptides
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1