Journal
FEBS LETTERS
Volume 583, Issue 19, Pages 3151-3157Publisher
WILEY
DOI: 10.1016/j.febslet.2009.09.020
Keywords
Prokaryotic ubiquitin-like protein; Mpa; ARC; Proteasome; NMR; Mycobacterium tuberculosis
Funding
- Swiss National Science Foundation (SNF)
- National Center for Excellence in Research (NCCR) Structural Biology program of the SNF
- ETH
- Fonds der Chemischen Industrie
Ask authors/readers for more resources
The mycobacterial ubiquitin-like protein Pup is coupled to proteins, thereby rendering them as substrates for proteasome-mediated degradation. The Pup-tagged proteins are recruited by the proteasomal ATPase Mpa (also called ARC). Using a combination of biochemical and NMR methods, we characterize the structural determinants of Pup and its interaction with Mpa, demonstrating that Pup adopts a range of extended conformations with a short helical stretch in its C-terminal portion. We show that the N-terminal coiled-coil domain of Mpa makes extensive contacts along the central region of Pup leaving its N-terminus unconstrained and available for other functional interactions. Structured summary: MINT-7262427:pup (uniprotkb:B6DAC1) binds (MI:0407) to mpa (uniprotkb:Q0G9Y7) by pull down (MI:0096) MINT-7262440:mpa (uniprotkb:Q0G9Y7) and pup (uniprotkb:B6DAC1) bind (MI:0407) by isothermal titration calorimetry (MI:0065) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available