Bhaskarla, Chetana and Bhosale, Manoj and Banerjee, Pip and Chandra, Nagasuma and Nandi, Dipankar (2018) Protein Tagging, Destruction and Infection. In: CURRENT PROTEIN & PEPTIDE SCIENCE, 19 (2). pp. 155-171.
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Cells possess protein quality control mechanisms to maintain proper cellular homeostasis. In eukaryotes, the roles of the ubiquitination and proteasome-mediated degradation of cellular proteins is well established. Recent studies have elucidated protein tagging mechanisms in prokaryotes, involving transfer messenger RNA (tmRNA) and pupylation. In this review, newer insights and bioinformatics analysis of two distinct bacterial protein tagging machineries are discussed. The machinery for tmRNA-mediated tagging is present in several eubacterial representatives, e.g. Escherichia coli, Mycobacterium tuberculosis, Bacillus subtilis etc., but not in two archaeal representatives, such as Thermoplasma acidophilum and Sulfolobus solfataricus. On the other hand, the machinery involving tagging with the prokaryotic ubiquitin-like protein (Pup) is absent in most bacteria but is encoded in some eubacterial representatives, e.g. Mycobacterium tuberculosis and Mycobacterium leprae. Furthermore, molecular details on the relationship between protein tagging and enzymes involved in protein degradation in bacteria during infection are emerging. Several pathogenic bacteria that do not express the major ATP-dependent proteases, Lon and Caseinolytic protease (ClpP), are avirulent. Also, some ATP-independent peptidases, such as PepA and PepN, modulate the infection process. The roles of bacterial proteins involved in tagging and degradation during infection are discussed. These aspects add a new dimension to better understanding of the peculiarities of host-pathogen interactions.
| Item Type: | Journal Article |
|---|---|
| Publication: | CURRENT PROTEIN & PEPTIDE SCIENCE |
| Publisher: | 10.2174/1389203718666170713100627 |
| Additional Information: | Copy right for this article belongs to the BENTHAM SCIENCE PUBL LTD, EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES |
| Department/Centre: | Division of Biological Sciences > Biochemistry |
| Date Deposited: | 12 Jan 2018 09:27 |
| Last Modified: | 12 Jan 2018 09:27 |
| URI: | http://eprints.iisc.ac.in/id/eprint/58663 |
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