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Side-by-side comparison of AP-MS, Tri-functional affinity probe, BioID, PUP-IT and SPIDER to identify CheZ-interacting proteins

ABSTRACT: Comparison of CheZ interactors’ ratio of two replicate experiments using five different methods, i.e., Affinity-Purification, Tri-functional affinity probe Sulfo-SBED and proximity labeling methods BioID, SPIDER, PUP-IT

ORGANISM(S): Escherichia Coli

SUBMITTER: Shengce Tao

PROVIDER: PXD037952 | iProX | Thu Nov 03 00:00:00 GMT 2022

REPOSITORIES: iProX

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Specific pupylation as IDEntity reporter (SPIDER) for the identification of protein-biomolecule interactions.

Jiang He-Wei HW Chen Hong H Zheng Yun-Xiao YX Wang Xue-Ning XN Meng Qingfeng Q Xie Jin J Zhang Jiong J Zhang ChangSheng C Xu Zhao-Wei ZW Chen Zi-Qing ZQ Wang Lei L Kong Wei-Sha WS Zhou Kuan K Ma Ming-Liang ML Zhang Hai-Nan HN Guo Shu-Juan SJ Xue Jun-Biao JB Hou Jing-Li JL Liu Zhe-Yi ZY Niu Wen-Xue WX Wang Fang-Jun FJ Wang Tao T Li Wei W Wang Rui-Na RN Dang Yong-Jun YJ Czajkowsky Daniel M DM Pei JianFeng J Dong Jia-Jia JJ Tao Sheng-Ce SC

Science China. Life sciences 20230414 8

Protein-biomolecule interactions play pivotal roles in almost all biological processes. For a biomolecule of interest, the identification of the interacting protein(s) is essential. For this need, although many assays are available, highly robust and reliable methods are always desired. By combining a substrate-based proximity labeling activity from the pupylation pathway of Mycobacterium tuberculosis and the streptavidin (SA)-biotin system, we developed the Specific Pupylation as IDEntity Repor ...[more]

PMID: 37059927

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