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Protein Turnover in Mycobacterial Proteomics
Understanding the biology of Mycobacterium tuberculosis is one of the primary challenges in current tuberculosis research. Investigation of mycobacterial biology using the systems biology approach has deciphered much information with regard to the bacilli and tuberculosis pathogenesis. The modulatio...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6254974/ https://www.ncbi.nlm.nih.gov/pubmed/19783922 http://dx.doi.org/10.3390/molecules14093237 |
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author | Rao, Prahlad K. Li, Qingbo |
author_facet | Rao, Prahlad K. Li, Qingbo |
author_sort | Rao, Prahlad K. |
collection | PubMed |
description | Understanding the biology of Mycobacterium tuberculosis is one of the primary challenges in current tuberculosis research. Investigation of mycobacterial biology using the systems biology approach has deciphered much information with regard to the bacilli and tuberculosis pathogenesis. The modulation of its environment and the ability to enter a dormant phase are the hallmarks of M. tuberculosis. Until now, proteome studies have been able to understand much about the role of various proteins, mostly in growing M. tuberculosis cells. It has been difficult to study dormant M. tuberculosis by conventional proteomic techniques with very few proteins being found to be differentially expressed. Discrepancy between proteome and transcriptome studies lead to the conclusion that a certain aspect of the mycobacterial proteome is not being explored. Analysis of protein turnover may be the answer to this dilemma. This review, while giving a gist of the proteome response of mycobacteria to various stresses, analyzes the data obtained from abundance studies versus data from protein turnover studies in M. tuberculosis. This review brings forth the point that protein turnover analysis is capable of discerning more subtle changes in protein synthesis, degradation, and secretion activities. Thus, turnover studies could be incorporated to provide a more in-depth view into the proteome, especially in dormant or persistent cells. Turnover analysis might prove helpful in drug discovery and a better understanding of the dynamic nature of the proteome of mycobacteria. |
format | Online Article Text |
id | pubmed-6254974 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Molecular Diversity Preservation International |
record_format | MEDLINE/PubMed |
spelling | pubmed-62549742018-11-30 Protein Turnover in Mycobacterial Proteomics Rao, Prahlad K. Li, Qingbo Molecules Review Understanding the biology of Mycobacterium tuberculosis is one of the primary challenges in current tuberculosis research. Investigation of mycobacterial biology using the systems biology approach has deciphered much information with regard to the bacilli and tuberculosis pathogenesis. The modulation of its environment and the ability to enter a dormant phase are the hallmarks of M. tuberculosis. Until now, proteome studies have been able to understand much about the role of various proteins, mostly in growing M. tuberculosis cells. It has been difficult to study dormant M. tuberculosis by conventional proteomic techniques with very few proteins being found to be differentially expressed. Discrepancy between proteome and transcriptome studies lead to the conclusion that a certain aspect of the mycobacterial proteome is not being explored. Analysis of protein turnover may be the answer to this dilemma. This review, while giving a gist of the proteome response of mycobacteria to various stresses, analyzes the data obtained from abundance studies versus data from protein turnover studies in M. tuberculosis. This review brings forth the point that protein turnover analysis is capable of discerning more subtle changes in protein synthesis, degradation, and secretion activities. Thus, turnover studies could be incorporated to provide a more in-depth view into the proteome, especially in dormant or persistent cells. Turnover analysis might prove helpful in drug discovery and a better understanding of the dynamic nature of the proteome of mycobacteria. Molecular Diversity Preservation International 2009-08-28 /pmc/articles/PMC6254974/ /pubmed/19783922 http://dx.doi.org/10.3390/molecules14093237 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Rao, Prahlad K. Li, Qingbo Protein Turnover in Mycobacterial Proteomics |
title | Protein Turnover in Mycobacterial Proteomics |
title_full | Protein Turnover in Mycobacterial Proteomics |
title_fullStr | Protein Turnover in Mycobacterial Proteomics |
title_full_unstemmed | Protein Turnover in Mycobacterial Proteomics |
title_short | Protein Turnover in Mycobacterial Proteomics |
title_sort | protein turnover in mycobacterial proteomics |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6254974/ https://www.ncbi.nlm.nih.gov/pubmed/19783922 http://dx.doi.org/10.3390/molecules14093237 |
work_keys_str_mv | AT raoprahladk proteinturnoverinmycobacterialproteomics AT liqingbo proteinturnoverinmycobacterialproteomics |