A synthetic biology approach for identifying de-SUMOylation enzymes of substrates

Junwen Huang; Junjie Huang; Jiayuan Wu; Mi Zhou; Siyi Luo; Jieming Jiang; Tongsheng Chen; Ling Shao; Jianbin Lai; Chengwei Yang

doi:10.1111/jipb.13838

A synthetic biology approach for identifying de-SUMOylation enzymes of substrates

J Integr Plant Biol. 2025 May;67(5):1211-1213. doi: 10.1111/jipb.13838. Epub 2025 Jan 21.

Authors

Junwen Huang^{1

2}, Junjie Huang^{1

3}, Jiayuan Wu¹, Mi Zhou¹, Siyi Luo¹, Jieming Jiang¹, Tongsheng Chen³, Ling Shao², Jianbin Lai¹, Chengwei Yang¹

Affiliations

¹ Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Sciences, South China Normal University, Guangzhou, 510631, China.
² School of Life Sciences, Zhaoqing University, Zhaoqing, 526061, China.
³ MOE Key Laboratory of Laser Life Science & Institute of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China.

PMID: 39835880
DOI: 10.1111/jipb.13838

Abstract

A synthetic biology approach using a robust reconstitution system in Escherichia coli enables the identification of plant ubiquitin-like proteases responsible for removing the small ubiquitin-like modifier (SUMO) post-translational modifications from specific protein substrates.

MeSH terms

Escherichia coli / genetics
Escherichia coli / metabolism
Protein Processing, Post-Translational
Substrate Specificity
Sumoylation*
Synthetic Biology* / methods

Abstract

MeSH terms

Grants and funding