Prokaryotic Ubiquitin-Like Protein Provides a Two-Part Degron to Mycobacterium Proteasome Substrates-Reference-Cited by-同舟云学术

Prokaryotic Ubiquitin-Like Protein Provides a Two-Part Degron to Mycobacterium Proteasome Substrates

Published:2010-06 Issue:11 Volume:192 Page:2933-2935
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Burns Kristin E.¹,Pearce Michael J.¹,Darwin K. Heran¹

Affiliation:

1. New York University School of Medicine Department of Microbiology, 550 First Avenue, MSB 236, New York, New York 10016

Abstract

ABSTRACT Prokaryotic ubiquitin-like protein (Pup) is a posttranslational modifier that targets proteins for degradation by the mycobacterial proteasome. We show that the disordered amino terminus of Pup is required for degradation, while the helical carboxyl terminus mediates its attachment to proteins. Thus, Pup has distinct regions that either interact with pupylation enzymes or initiate proteasomal degradation.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.01639-09

Reference20 articles.

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2. Cerda-Maira, F., and K. H. Darwin. 2009. The Mycobacterium tuberculosis proteasome: more than just a barrel-shaped protease. Microbes Infect. 11 : 1150-1155.

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4. Chen, X., W. C. Solomon, Y. Kang, F. Cerda-Maira, K. H. Darwin, and K. J. Walters. 2009. Prokaryotic ubiquitin-like protein pup is intrinsically disordered. J. Mol. Biol. 392 : 208-217.

5. Darwin, K. H. 2009. Prokaryotic ubiquitin-like protein, proteasomes, and pathogenesis. Nat. Rev. Microbiol. 7 : 485-491.

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