The prokaryotic ubiquitin-like protein presents poor cleavage sites for proteasomal degradation

Zerbib, Erez; Schlussel, Shai; Hecht, Nir; Bagdadi, Noy; Eichler, Jerry; Gur, Eyal

doi:10.1016/j.celrep.2021.109428

Cited by 2 publications

(1 citation statement)

References 50 publications

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“…Finally, these authors used the molecular mass of covalent modification to identify a Pup substrate (SHJG_3659) [ 77 ]. The depupylation function of Dop has also been confirmed in other microorganisms and is not explored further in this study [ 78 , 79 ]. When Pup is deamidated, it will hydrolyze ATP under the action of PafA and catalyze the phosphorylation of Glu [ 80 ], forming an intermediate that is connected to the substrate Lys [ 81 ].…”

Section: Proteasomementioning

confidence: 96%

Degradation Mechanism of AAA+ Proteases and Regulation of Streptomyces Metabolism

Gao

et al. 2022

Biomolecules

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Hundreds of proteins work together in microorganisms to coordinate and control normal activity in cells. Their degradation is not only the last step in the cell’s lifespan but also the starting point for its recycling. In recent years, protein degradation has been extensively studied in both eukaryotic and prokaryotic organisms. Understanding the degradation process is essential for revealing the complex regulatory network in microorganisms, as well as further artificial reconstructions and applications. This review will discuss several studies on protein quality-control family members Lon, FtsH, ClpP, the proteasome in Streptomyces, and a few classical model organisms, mainly focusing on their structure, recognition mechanisms, and metabolic influences.

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