Recent developments in the analysis of protein complexes.
The goal of this review is to analyse how recent technical developments contributed to the biochemical characterisation of protein complexes. Improvement of tags used for protein purification, including in our own laboratory, and the development of new strategies have allowed the use of generic procedures for the purification of a wide variety of protein complexes. Together with increased mass spectrometry sensitivity and automation, this made high throughput studies of protein complexes possible and allowed proteome-wide analyses of protein complexes. However, knowledge of protein complex composition, even at the cellular level, will not be sufficient to understand their function. We suggest that the next level of analysis in this area will be the definition of internal subunit arrangement in complexes as a first step toward more detailed structural analyses.
Dziembowski
Andrzej
A
Equipe Labelisée 'La Ligue', Centre de Génétique Moléculaire, CNRS UPR 2167 Associated with University Paris 6, Avenue de la Terrasse, 91198 Cedex, Gif sur Yvette, France.
Séraphin
Bertrand
B
D000345:Affinity Labels; D000818:Animals; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D025941:Protein Interaction Mapping / Q000379:methods; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics; D020798:Two-Hybrid System Techniques
D000345:Affinity Labels; D011506:Proteins