New chemical crosslinking methods for the identification of transient protein-protein interactions with multiprotein complexes.
Most proteins function as multiprotein complexes or interact with multiprotein complexes. Identification of protein-protein interactions in the context of their physiologically relevant complexes is therefore key to fully understand the cellular machinery. Here I discuss advances in chemical crosslinking methods that allow investigators to map direct subunit contacts in transient interactions with multimeric complexes. Methods discussed fall into two categories: (i) in vitro approaches with localized, inducible crosslinking reagents and (ii) in vivo approaches with unlocalized crosslinkers.
Institut für Mikrobiologie, Biozentrum, Goethe Universität, Marie-Curie-St. 9, N250, 60439 Frankfurt am Main, Germany. k.melcher@ulster.ac.uk.
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D000818:Animals; D047369:Chromatin Immunoprecipitation; D003432:Cross-Linking Reagents / Q000737:chemistry*; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism*; D010777:Photochemistry; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism
D003432:Cross-Linking Reagents; D046912:Multiprotein Complexes; D011506:Proteins; D014157:Transcription Factors