ArticleCellular and molecular life sciences : CMLS2016
Femtosecond UV-laser pulses to unveil protein-protein interactions in living cells.
Article in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Next-generation sequencing: A new avenue to understand viral RNA-protein interactions.The Journal of biological chemistry · 2022Review
- RNA binding of Hfq monomers promotes RelA-mediated hexamerization in a limiting Hfq environment.Nature communications · 2021Article
- FAX-RIC enables robust profiling of dynamic RNP complex formation in multicellular organisms in vivo.Nucleic acids research · 2021Article
- Article
- Proteomic fingerprints of damage in extracellular matrix assemblies.Matrix biology plus · 2020Article
- Characterization of Ultraviolet Photoreactions in Therapeutic Peptides by Femtosecond Laser Catalysis and Mass Spectrometry.ACS omega · 2019Article
- Characterization of a Surface-Active Protein Extracted from a Marine Strain ofInternational journal of molecular sciences · 2019Article
- Effects of amino acids on the lignocellulose degradation byBiotechnology for biofuels · 2019Article
- An Oligonucleotide-based Tandem RNA Isolation Procedure to Recover Eukaryotic mRNA-Protein Complexes.Journal of visualized experiments : JoVE · 2018Article
- Identification of peptide-binding sites within BSA using rapid, laser-induced covalent cross-linking combined with high-performance mass spectrometry.Journal of molecular recognition : JMR · 2018Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A hallmark to decipher bioprocesses is to characterize protein-protein interactions in living cells. To do this, the development of innovative methodologies, which do not alter proteins and their natural environment, is particularly needed. Here, we report a method (LUCK, Laser UV Cross-linKing) to in vivo cross-link proteins by UV-laser irradiation of living cells. Upon irradiation of HeLa cells under controlled conditions, cross-linked products of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were detected, whose yield was found to be a linear function of the total irradiation energy. We demonstrated that stable dimers of GAPDH were formed through intersubunit cross-linking, as also observed when the pure protein was irradiated by UV-laser in vitro. We proposed a defined patch of aromatic residues located at the enzyme subunit interface as the cross-linking sites involved in dimer formation. Hence, by this technique, UV-laser is able to photofix protein surfaces that come in direct contact. Due to the ultra-short time scale of UV-laser-induced cross-linking, this technique could be extended to weld even transient protein interactions in their native context.
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