Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
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- 作者：Jonas Barandun ; Fred F. Damberger ; Cyrille L. Delley…
- 关键词：Pupylation ; Prokaryotic ubiquitin ; like protein Pup ; Mycobacterium tuberculosis ; NMR ; Intrinsically disordered proteins
- 刊名：BMC Structural Biology
- 出版年：2018
- 出版时间：January 2018
- 年：0
- 卷：17
- 期：1
- 全文大小：3548KB
- 刊物主题：Biochemistry, general; Protein Science; Crystallography and Scattering Methods; Mass Spectrometry; Spectroscopy/Spectrometry;
- 出版者：BioMed Central
- ISSN：1472-6807
- 卷排序：17
文摘
BackgroundThe post-translational modification pathway referred to as pupylation marks proteins for proteasomal degradation in Mycobacterium tuberculosis and other actinobacteria by covalently attaching the small protein Pup (prokaryotic ubiquitin-like protein) to target lysine residues. In contrast to the functionally analogous eukaryotic ubiquitin, Pup is intrinsically disordered in its free form. Its unfolded state allows Pup to adopt different structures upon interaction with different binding partners like the Pup ligase PafA and the proteasomal ATPase Mpa. While the disordered behavior of free Pup has been well characterized, it remained unknown whether Pup adopts a distinct structure when attached to a substrate.