Ubiquitin is a small protein that exists in all eukaryotic cells. It performs its myriad functions through conjugation to a large range of target proteins. A variety of different modifications can occur. The ubiquitin protein itself consists of 76 amino acids and has a …

The biological functions of many proteins are altered by their covalent attachment to polypeptide modifiers. The best-known example of this type of modification is ubiquitination. Ubiquitin has a well-documented role in targeting proteins for degradation …

It has been shown that altering the C-terminal residue of ubiquitin from glycine to valine (Ub G76V) creates a form of ubiquitin that cannot be cleaved by ubiquitin C-terminal hydrolases 7,13.

2021年1月14日 · Ubiquitin modifications control a plethora of vital cellular processes through proteolytic and nonproteolytic mechanisms, including proteasomal degradation and proteostasis,...

Our results suggest that ubiquitin not only serves as a recognition tag but also assists degradation by facilitating protein unfolding. Results and Discussion Ubiquitination of Ubc7, Which Mediates its Proteasomal Degradation, Leads to Thermal Destabilization and Local Structural Unwinding.

The covalent attachment of ubiquitin to a target protein is achieved through the sequential action of three types of enzymes: E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin ligase). Ubiquitination operates as a molecular tag capable of modifying the target protein's function, localization, or fate.

Ubiquitin is a small polypeptide that functions as a molecular tag to mark proteins for degradation or to participate in various cellular processes such as DNA repair and protein localization. It is attached to proteins through a multistep enzymatic process called ubiquitination, involving enzymes known as E1, E2, and E3.

2023年12月15日 · Here, we introduce a set of engineered ubiquitin protein ligases and matching ubiquitin acceptor tags for the rapid, inducible linear (M1-), K48-, or K63-linked polyubiquitylation of proteins in yeast and mammalian cells.

2015年10月9日 · The specific topics addressed in this article include sample preparation, the separation, detection and identification of particular ubiquitin chains by immunoblotting, and the analysis of ubiquitin chain topology through the combined use of ubiquitin-binding proteins and ubiquitin linkage-specific deubiquitylases.

2024年10月3日 · Ubiquitin is a prevalent form of post-translational modification in eukaryotes that impacts a plethora of cellular process including protein turnover, DNA repair, and immune and stress responses. 2 Ubiquitin serves as a covalent tag for target proteins, and recognition of this tag regulates target clearance, localization, or function.