A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa

Sutter, Markus; Striebel, Frank; Damberger, Fred F.; Allain, Frédéric H.-T.; Weber-Ban, Eilika

doi:10.1016/j.febslet.2009.09.020

« Previous Next »FEBS Letters
Volume 583, Issue 19 , Pages 3151-3157, 6 October 2009

A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa

Edited by Miguel De la Rosa

ETH Zurich, Institute of Molecular Biology and Biophysics, Zurich, Switzerland

Received 8 July 2009; received in revised form 4 September 2009; accepted 8 September 2009. published online 15 September 2009.

Abstract

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)