Induced Folding Under Membrane Mimetic and Acidic Conditions Implies Undiscovered Biological Roles of Prokaryotic Ubiquitin-Like Protein Pup
| Autor: | Jigang Yu, Shanhui Liao, Xuecheng Zhang, Kaiqin Ye, Jiahai Zhang, Qiang Shang, Xiaoming Tu |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Folding Circular dichroism Magnetic Resonance Spectroscopy Protein subunit Plasma protein binding Biochemistry Protein Structure Secondary 03 medical and health sciences Protein structure Bacterial Proteins Ubiquitin Structural Biology Prokaryotic ubiquitin-like protein Ubiquitins Micelles Adenosine Triphosphatases Binding Sites biology Circular Dichroism Sodium Dodecyl Sulfate Mycobacterium tuberculosis General Medicine Hydrogen-Ion Concentration Surface Plasmon Resonance 030104 developmental biology Proteasome biology.protein Biophysics Protein folding Acids Protein Binding |
| Zdroj: | Protein & Peptide Letters. 23:756-762 |
| ISSN: | 0929-8665 |
| DOI: | 10.2174/0929866523666160530185322 |
| Popis: | Ubiquitin-like proteins play important roles in diverse biological processes. In Mycobacterium tuberculosis, Pup (prokaryotic ubiquitin-like protein), a functional homologue of eukaryotic ubiquitin, interacts with the proteasome ATPase subunit Mpa to recognize and unfold substrates, and then translocate them into the proteasome core for degradation. Previous studies revealed that, Pup, an intrinsically disordered protein (IDP), adopts a helical structure upon binding to the N-terminal coiled-coil domain of Mpa, at its disordered C-terminal region. In the present study, using circular dichroism (CD), surface plasmon resonance (SPR) and nuclear magnetic resonance (NMR), we show that membrane mimetic and acidic conditions also induce Pup to adopt helical conformations. Moreover, at low pH, Pup, via both of its N- and C-terminal regions, binds to Mpa on sites from the N-terminal region in addition to the C-terminal region of the coiled-coil domain. Our results imply Pup may play undiscovered roles in some biological processes e.g. those involve in membrane. |
| Databáze: | OpenAIRE |
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