The PIN-domain toxin–antitoxin array in mycobacteria

• Published in: Trends in microbiology (Regular ed.) 2005-08, Vol.13 (8), p.360-365
• Main Authors: Arcus, Vickery L., Rainey, Paul B., Turner, Susan J.
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Adenosine Triphosphatases - physiology; Amino Acid Sequence; Antitoxins - physiology; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Models, Molecular; Molecular Motor Proteins - genetics; Molecular Motor Proteins - metabolism; Molecular Motor Proteins - physiology; Molecular Sequence Data; Mycobacterium tuberculosis; Mycobacterium tuberculosis - genetics; Mycobacterium tuberculosis - metabolism; Mycobacterium tuberculosis - physiology; Operon; Protein Structure, Tertiary; Sequence Alignment
• ISSN: 0966-842X; 1878-4380
• DOI: 10.1016/j.tim.2005.06.008

PIN-domains (homologues of the pilT N-terminal domain) are small protein domains of ∼140 amino acids. They are found in a diverse range of organisms and recent evidence from bioinformatics, biochemistry, structural biology and microbiology suggest that the majority of the prokaryotic PIN-domain proteins are the toxic components of toxin-antitoxin (TA) operons. Several microorganisms have a large cohort of these operons. For example, the genome of Mycobacterium tuberculosis encodes 48 PIN-domain proteins, of which 38 are thought to be involved in TA interactions. This large array of PIN-domain TA operons raises questions as to their evolutionary origin and contemporary functional significance. We suggest that the evolutionary origin of genes encoding mycobacterial PIN-domain TA operons is linked to the mobile gene pool, but that TA operons can become resident within the chromosome of host cells from where they might be recruited to fulfil a variety of roles associated with retardation of cell growth and persistence in stressful environments.