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Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond

https://doi.org/10.1124/pr.118.015651

Zhao, Bo; Tsai, Yien Che; Jin, Bo; Wang, Bufan; Wang, Yiyang; Zhou, Han; Carpenter, Tomaya; Weissman, Allan M.; Yin, Jun; D. Ye, Richard (February 2020, Pharmacological Reviews)

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Enhancing the incorporation of lysine derivatives into proteins with methylester forms of unnatural amino acids

https://doi.org/10.1016/j.bmcl.2019.126876

Zhou, Han; Cheung, Jenny W.; Carpenter, Tomaya; Jones, Stacey K.; Luong, Nhu H.; Tran, Nhi C.; Jacobs, Savannah E.; Galbada Liyanage, Sahan A.; Cropp, T. Ashton; Yin, Jun (January 2020, Bioorganic & Medicinal Chemistry Letters)

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Linkage‐Specific Synthesis of Di‐ubiquitin Probes Enabled by the Incorporation of Unnatural Amino Acid ThzK

https://doi.org/10.1002/cbic.202200133

Zhou, Han; Carpenter, Tomaya; Fu, Xuan; Jin, Bo; Ody, Britton; Hassan, Mohammad_Sazid; Jacobs, Savannah_E; Cheung, Jenny; Nicholson, Eve_M; Turlington, Mark; et al (March 2022, ChemBioChem)

Abstract Di‐ubiquitin (diUB) conjugates of defined linkages are useful tools for probing the functions of UB ligases, UB‐binding proteins and deubiquitinating enzymes (DUBs) in coding, decoding and editing the signals carried by the UB chains. Here we developed an efficient method for linkage‐specific synthesis of diUB probes based on the incorporation of the unnatural amino acid (UAA)N^ϵ‐L‐thiaprolyl‐L‐Lys (L‐ThzK) into UB for ligation with another UB at a defined Lys position. The diUB formed by the UAA‐mediated ligation reaction has a G76C mutation on the side of donor UB for conjugation with E2 and E3 enzymes or undergoing dethiolation to generate a covalent trap for DUBs. The development of UAA mutagenesis for diUB synthesis provides an easy route for preparing linkage‐specific UB‐based probes to decipher the biological signals mediated by protein ubiquitination.
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