Recent developments in the analysis of protein complexes

被引:72
|
作者
Dziembowski, A [1 ]
Séraphin, B [1 ]
机构
[1] Univ Paris 06, CNRS UPR 2167, Equipe Labelisee La Ligue, Ctr Genet Mol, F-91198 Gif Sur Yvette, France
关键词
protein interaction; protein purification; mass spectrometry; tandem affinity purification; yeast two-hybrid; protein cross-linking;
D O I
10.1016/S0014-5793(03)01357-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:1 / 6
页数:6
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