CHEMICAL CROSS-LINKING;
INDEPENDENT PROTEASOMAL DEGRADATION;
QUANTITATIVE PROTEOMICS REVEALS;
NONCOVALENT PROTEIN COMPLEXES;
20S PROTEASOME;
ABSOLUTE QUANTIFICATION;
ELECTROSPRAY-IONIZATION;
26S PROTEASOME;
CRYSTAL-STRUCTURE;
YEAST;
D O I:
10.1017/S0033583516000160
中图分类号:
Q6 [生物物理学];
学科分类号:
071011 ;
摘要:
Protein complexes form the critical foundation for a wide range of biological process, however understanding the intricate details of their activities is often challenging. In this review we describe how mass spectrometry (MS) plays a key role in the analysis of protein assemblies and the cellular pathways which they are involved in. Specifically, we discuss how the versatility of mass spectrometric approaches provides unprecedented information on multiple levels. We demonstrate this on the ubiquitin-proteasome proteolytic pathway, a process that is responsible for protein turnover. We follow the various steps of this degradation route and illustrate the different MS workflows that were applied for elucidating molecular information. Overall, this review aims to stimulate the integrated use of multiple mass spectrometry approaches for analyzing complex biological systems.