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Survival of mycobacteria depends on proteasome-mediated amino acid recycling under nutrient limitation.
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- المؤلفون: Elharar, Yifat1; Roth, Ziv1,2; Hermelin, Inna1; Moon, Alexandra1; Peretz, Gabriella1,2; Shenkerman, Yael1; Vishkautzan, Marina1,2; Khalaila, Isam3; Gur, Eyal1,2
- المصدر:
EMBO Journal. 8/18/2014, Vol. 33 Issue 16, p1802-1814. 13p. 5 Diagrams, 4 Graphs.
- الموضوع:
- معلومة اضافية
- نبذة مختصرة :
Intracellular protein degradation is an essential process in all life domains. While in all eukaryotes regulated protein degradation involves ubiquitin tagging and the 26S-proteasome, bacterial prokaryotic ubiquitin-like protein (Pup) tagging and proteasomes are conserved only in species belonging to the phyla Actinobacteria and Nitrospira. In Mycobacterium tuberculosis, the Pup-proteasome system (PPS) is important for virulence, yet its physiological role in non-pathogenic species has remained an enigma. We now report, using Mycobacterium smegmatis as a model organism, that the PPS is essential for survival under starvation. Upon nitrogen limitation, PPS activity is induced, leading to accelerated tagging and degradation of many cytoplasmic proteins. We suggest a model in which the PPS functions to recycle amino acids under nitrogen starvation, thereby enabling the cell to maintain basal metabolic activities. We also find that the PPS auto-regulates its own activity via pupylation and degradation of its components in a manner that promotes the oscillatory expression of PPS components. As such, the destructive activity of the PPS is carefully balanced to maintain cellular functions during starvation. [ABSTRACT FROM AUTHOR]
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