Pupylation-dependent and -independent proteasomal degradation in mycobacteria

Biomolecular Concepts
Frank ImkampJonas Barandun

Abstract

Bacteria make use of compartmentalizing protease complexes, similar in architecture but not homologous to the eukaryotic proteasome, for the selective and processive removal of proteins. Mycobacteria as members of the actinobacteria harbor proteasomes in addition to the canonical bacterial degradation complexes. Mycobacterial proteasomal degradation, although not essential during normal growth, becomes critical for survival under particular environmental conditions, like, for example, during persistence of the pathogenic Mycobacterium tuberculosis in host macrophages or of environmental mycobacteria under starvation. Recruitment of protein substrates for proteasomal degradation is usually mediated by pupylation, the post-translational modification of lysine side chains with the prokaryotic ubiquitin-like protein Pup. This substrate recruitment strategy is functionally reminiscent of ubiquitination in eukaryotes, but is the result of convergent evolution, relying on chemically and structurally distinct enzymes. Pupylated substrates are recognized by the ATP-dependent proteasomal regulator Mpa that associates with the 20S proteasome core. A pupylation-independent proteasome degradation pathway has recently been discovered that is...Continue Reading

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Citations

Aug 9, 2016·Journal of Molecular Biology·Ofir RegevEyal Gur
Oct 27, 2017·Scientific Reports·Begonia Fudrini OlivenciaFrank Imkamp
Mar 18, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Kaja RožmanStanislav Gobec
Jan 8, 2021·PLoS Pathogens·Kathleen R NicholsonPatricia A Champion
May 25, 2021·Frontiers in Molecular Biosciences·Matylda Anna IzertMaria Wiktoria Górna

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