Femtosecond UV-laser pulses to unveil protein–protein interactions in living cells

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• 作者：Francesco Itri ; Daria M. Monti…
• 关键词：Protein–protein interactions ; Ultra ; short UV ; laser pulses ; UV cross ; linking ; Living cells irradiation
• 刊名：Cellular and Molecular Life Sciences (CMLS)
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：73
• 期：3
• 页码：637-648
• 全文大小：3,018 KB
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• 作者单位：Francesco Itri (1)
  Daria M. Monti (1) (2)
  Bartolomeo Della Ventura (3)
  Roberto Vinciguerra (1)
  Marco Chino (1)
  Felice Gesuele (3)
  Angelina Lombardi (1)
  Raffaele Velotta (3) (4)
  Carlo Altucci (3) (4)
  Leila Birolo (1)
  Renata Piccoli (1) (2)
  Angela Arciello (1) (2)
  
  1. Department of Chemical Sciences, University of Naples Federico II, 80126, Naples, Italy
  2. Istituto Nazionale di Biostrutture e Biosistemi (INBB), Rome, Italy
  3. Department of Physics, University of Naples Federico II, 80126, Naples, Italy
  4. Consorzio Nazionale Interuniversitario per le Scienze Fisiche della Materia (CNISM), UdR, Naples, Italy
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Cell Biology
  Biomedicine
  Life Sciences
  Biochemistry
  
• 出版者：Birkh盲user Basel
• ISSN：1420-9071

文摘

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. Keywords Protein–protein interactions Ultra-short UV-laser pulses UV cross-linking Living cells irradiation