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Super-resolution proximity labeling with enhanced direct identification of biotinylation sites

Cited 1 time in Web of Science Cited 1 time in Scopus
Authors

Shin, Sanghee; Lee, Song-Yi; Kang, Myeong-Gyun; Jang, Dong-Gi; Kim, Jeesoo; Rhee, Hyun-Woo; Kim, Jong-Seo

Issue Date
2024-05
Publisher
Nature Research
Citation
Communications Biology, Vol.7 No.1, p. 554
Abstract
Promiscuous labeling enzymes, such as APEX2 or TurboID, are commonly used in in situ biotinylation studies of subcellular proteomes or protein–protein interactions. Although the conventional approach of enriching biotinylated proteins is widely implemented, in-depth identification of specific biotinylation sites remains challenging, and current approaches are technically demanding with low yields. A novel method to systematically identify specific biotinylation sites for LC-MS analysis followed by proximity labeling showed excellent performance compared with that of related approaches in terms of identification depth with high enrichment power. The systematic identification of biotinylation sites enabled a simpler and more efficient experimental design to identify subcellular localized proteins within membranous organelles. Applying this method to the processing body (PB), a non-membranous organelle, successfully allowed unbiased identification of PB core proteins, including novel candidates. We anticipate that our newly developed method will replace the conventional method for identifying biotinylated proteins labeled by promiscuous labeling enzymes.
ISSN
2399-3642
URI
https://hdl.handle.net/10371/203140
DOI
https://doi.org/10.1038/s42003-024-06112-w
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Molecular Interactomics, Proteomics, Systems Biology, 단백체학, 분자상호작용체학, 시스템생물학

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