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Chapter 16 : The Proteome of

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The Proteome of , Page 1 of 2

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Abstract:

The ultimate goal of studying the proteome of is to identify the many proteins that comprise the bacillus and to understand how they behave in concert with each other. This chapter provides an overview of the current understanding of the proteome, including unique aspects, and a description of the approaches being applied. The application of more comprehensive proteomics techniques to was pioneered by Sadamu Nagai. is able to persist in a latent state for long periods under conditions characterized by low oxygen levels, low pH, and nutrient deprivation. In bacteria, proteins are localized to their extracytoplasmic compartments through active protein export systems that selectively translocate the appropriate proteins out of the cytoplasm. As virulence factors and protective antigens are among the exported proteins of , the protein export systems of are important not only to the physiology of the bacillus but also to pathogenesis of disease. The Sec pathway is essential, highly conserved, and the primary pathway for protein transport across the cytoplasmic membrane of bacteria. Annotation of the genome and two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) analyses provides a rough template of proteome function and composition. Application of proteomic techniques to the global identification of posttranslational modifications in has yet to be undertaken and is warranted in the coming phase of proteome research.

Citation: Belisle J, Braunstein M, Rosenkrands I, Andersen P. 2005. The Proteome of , p 235-260. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch16
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Figure 1a

2-D PAGE of the culture filtrate (A), cytosol (B), and cell wall (C) proteins of H37Rv. Reprinted from reference 165 with permission.

Citation: Belisle J, Braunstein M, Rosenkrands I, Andersen P. 2005. The Proteome of , p 235-260. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch16
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Image of Figure 1b
Figure 1b

2-D PAGE of the culture filtrate (A), cytosol (B), and cell wall (C) proteins of H37Rv. Reprinted from reference 165 with permission.

Citation: Belisle J, Braunstein M, Rosenkrands I, Andersen P. 2005. The Proteome of , p 235-260. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch16
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Image of Figure 2
Figure 2

Schematic of the conserved ESAT-6 cluster region 1 of H37Rv. ORFs are depicted as black arrows showing the direction of transcription. The conserved genes in the cluster are boxed. The names of each ORF are listed above the diagram. Predicted transmembrane domains were identified with the Tmpred prediction software ( ).

Citation: Belisle J, Braunstein M, Rosenkrands I, Andersen P. 2005. The Proteome of , p 235-260. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch16
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Image of Figure 3
Figure 3

Triacylated Cys residue of the mature N terminus of the 19-kDa lipoprotein (LpqH [Rv3763]). R1, R2, and R3 indicate palmitic acid, palmitoleic acid, oleic acid, or tuberculostearic acid; with the acylation at each site presumably being heterogeneous.

Citation: Belisle J, Braunstein M, Rosenkrands I, Andersen P. 2005. The Proteome of , p 235-260. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch16
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Figure 4

Alignment of the glycosylation sites of Apa (Rv1860) and MBP83 (Rv2873). “Position” indicates the location of the peptide shown in the mature protein sequence.

Citation: Belisle J, Braunstein M, Rosenkrands I, Andersen P. 2005. The Proteome of , p 235-260. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch16
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