Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis.
Proteasomes are ATP-dependent, multisubunit proteases that are found in all eukaryotes and archaea and some bacteria. In eukaryotes, the small protein ubiquitin is covalently attached in a post-translational manner to proteins that are targeted for proteasomal degradation. Despite the presence of proteasomes in many prokaryotes, ubiquitin or other post-translational protein modifiers were presumed to be absent from these organisms. Recently a prokaryotic ubiquitin-like protein, Pup, was found to target proteins for proteolysis by the Mycobacterium tuberculosis proteasome. The discovery of this ubiquitin-like modifier opens up the possibility that other bacteria may also have small post-translational protein tagging systems, with the ability to affect cellular processes.
Darwin
K Heran
KH
Department of Microbiology, New York University School of Medicine, 550 First Avenue MSB 236, New York, New York 10016, USA. heran.darwin@med.nyu.edu
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D006801:Humans; D009169:Mycobacterium tuberculosis / Q000378:metabolism / Q000472:pathogenicity*; D011387:Prokaryotic Cells / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D014452:Ubiquitins / Q000378:metabolism*
D001426:Bacterial Proteins; D014452:Ubiquitins; D046988:Proteasome Endopeptidase Complex