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Spontaneous and specific chemical cross-linking in live cells to capture and identify protein interactions.

Abstract：

:Covalently locking interacting proteins in situ is an attractive strategy for addressing the challenge of identifying weak and transient protein interactions, yet it is demanding to execute chemical reactions in live systems in a biocompatible, specific, and autonomous manner. Harnessing proximity-enabled reactivity of an unnatural amino acid incorporated in the bait toward a target residue of unknown proteins, here we genetically encode chemical cross-linkers (GECX) to cross-link interacting proteins spontaneously and selectively in live cells. Obviating an external trigger for reactivity and affording residue specificity, GECX enables the capture of low-affinity protein binding (affibody with Z protein), elusive enzyme-substrate interaction (ubiquitin-conjugating enzyme UBE2D3 with substrate PCNA), and endogenous proteins interacting with thioredoxin in E. coli cells, allowing for mass spectrometric identification of interacting proteins and crosslinking sites. This live cell chemistry-based approach should be valuable for investigating currently intangible protein interactions in vivo for better understanding of biology in physiological settings.

journal_name

Nat Commun

journal_title

Nature communications

authors

Yang B,Tang S,Ma C,Li ST,Shao GC,Dang B,DeGrado WF,Dong MQ,Wang PG,Ding S,Wang L

doi

10.1038/s41467-017-02409-z

subject

Has Abstract

pub_date

2017-12-21 00:00:00

pages

2240

issue

1

issn

2041-1723

pii

10.1038/s41467-017-02409-z

journal_volume

8

pub_type

杂志文章

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