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Analysis of the proteome of Mycobacterium tuberculosis in silico
Open accessAbstract
Novel bioinformatics routines have been used to provide a more detailed definition of the proteome of Mycobacterium tuberculosis H37Rv. Over half of the current proteins result from gene duplication or domain shuffling events while one-sixth show no similarity to polypeptides described in other organisms. Prominent among the genes that appear to have been duplicated on numerous occasions are those involved in fatty acid metabolism, regulation of gene expression, and the unusually glycine-rich PE and PPE proteins. Protein similarity analysis, coupled with inspection of the genetic neighbourhood, was used to explore possible functional relatedness. This uncovered four large mce operons whose proteins may mediate initial interactions between the tubercle bacillus and host cells, together with a cluster of genes that might encode components of a structure required for secretion of ESAT-6 like proteins. Close linkage of the mmpL genes, encoding large membrane proteins, with those required for fatty acid metabolism suggests involvement in lipid transport. Compared to free-living bacteria, M. tuberculosis has a significantly smaller transport protein repertoire and this may reflect its intracellular lifestyle.
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“which were first discovered almost 20 years ago during in silico analyses of the genome sequence and the proteome of Mycobacterium tuberculosis H37Rv (17,18).”
From ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins (2019) · cites this paper as [18]
In the citing paper
“Five ESX systems are encoded in the genome of M. tuberculosis (16,18), and this number is the highest found in mycobacteria so far; other mycobacterial species show fewer systems (e.g., Mycobacterium marinum shows four systems and Mycobacterium abscessus shows three systems) (21,22).”
From ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins (2019) · cites this paper as [18]
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Metadata
- Authors
- Tekaia, F., Gordon, S. V., Garnier, T., Brosch, R., Barrell, B. G., & Cole, S. T.
- Affiliations
- Institut Pasteur (FR)
- Wellcome Sanger Institute (GB)
- Venue
- Tubercle and Lung Disease
- Publisher
- Elsevier BV
- Published
- 1999-12
- Volume
- 79
- Issue
- 6
- Pages
- 329-342
- ISSN
- 0962-8479 (ISSN-L)
- OpenAlex
- W2076379808
- Cited by
- 311
- References
- 59
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 5 · 2023: 5 · 2022: 6 · 2021: 8 · 2020: 4 · 2019: 13 · 2018: 4 · 2017: 6 · 2016: 12 · 2015: 15 · 2014: 17 · 2013: 15 · 2012: 18
- FWCI
- 11.60
- Type
- journal article
- Language
- en
- Open access
- green
- infoscience.epfl.ch
- Locations
- Tubercle and Lung Disease (publishedVersion)
- PubMed (publishedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, proteome, gene duplication, domain shuffling, fatty acid metabolism, gene expression regulation, host-pathogen interaction, lipid transport, membrane transporters, intracellular lifestyle
- MeSH terms
- Bacterial Proteins, Fatty Acids, Genes, Bacterial, Mycobacterium tuberculosis, Operon, Computational Biology, Genes, Duplicate, Proteome, Amino Acid Motifs
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