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

详细信息    查看全文

• 作者：Markus Sutter ; Frank Striebel ; Fred F. Damberger ; Fré ; dé ; ric H.-T. Allain ; Eilika Weber-Ban
• 关键词：Prokaryotic ubiquitin-like protein ; Mpa ; ARC ; Proteasome ; NMR ; Mycobacterium tuberculosis
• 刊名：FEBS Letters
• 出版年：2009
• 出版时间：6 October 2009
• 年：2009
• 卷：583
• 期：19
• 页码：3151-3157
• 全文大小：2134 K

文摘

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)