Top-down characterization of endogenous protein complexes with native proteomics. Skinner, O. S., Haverland, N. A., Fornelli, L., Melani, R. D., Do Vale, L. H. F., Seckler, H. S., Doubleday, P. F., Schachner, L. F., Srzentić, K., Kelleher, N. L., & Compton, P. D. Nature Chemical Biology, 14(1):36–41, January, 2018. ![Top-down characterization of endogenous protein complexes with native proteomics [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Protein complexes exhibit great diversity in protein membership, post-translational modifications and noncovalent cofactors, enabling them to function as the actuators of many important biological processes. The exposition of these molecular features using current methods lacks either throughput or molecular specificity, ultimately limiting the use of protein complexes as direct analytical targets in a wide range of applications. Here, we apply native proteomics, enabled by a multistage tandem MS approach, to characterize 125 intact endogenous complexes and 217 distinct proteoforms derived from mouse heart and human cancer cell lines in discovery mode. The native conditions preserved soluble protein–protein interactions, high-stoichiometry noncovalent cofactors, covalent modifications to cysteines, and, remarkably, superoxide ligands bound to the metal cofactor of superoxide dismutase 2. These data enable precise compositional analysis of protein complexes as they exist in the cell and demonstrate a new approach that uses MS as a bridge to structural biology.
@article{skinner_top-down_2018,
title = {Top-down characterization of endogenous protein complexes with native proteomics},
volume = {14},
copyright = {2017 Nature Publishing Group},
issn = {1552-4469},
url = {https://www.nature.com/articles/nchembio.2515},
doi = {10.1038/nchembio.2515},
abstract = {Protein complexes exhibit great diversity in protein membership, post-translational modifications and noncovalent cofactors, enabling them to function as the actuators of many important biological processes. The exposition of these molecular features using current methods lacks either throughput or molecular specificity, ultimately limiting the use of protein complexes as direct analytical targets in a wide range of applications. Here, we apply native proteomics, enabled by a multistage tandem MS approach, to characterize 125 intact endogenous complexes and 217 distinct proteoforms derived from mouse heart and human cancer cell lines in discovery mode. The native conditions preserved soluble protein–protein interactions, high-stoichiometry noncovalent cofactors, covalent modifications to cysteines, and, remarkably, superoxide ligands bound to the metal cofactor of superoxide dismutase 2. These data enable precise compositional analysis of protein complexes as they exist in the cell and demonstrate a new approach that uses MS as a bridge to structural biology.},
language = {en},
number = {1},
urldate = {2019-01-06TZ},
journal = {Nature Chemical Biology},
author = {Skinner, Owen S. and Haverland, Nicole A. and Fornelli, Luca and Melani, Rafael D. and Do Vale, Luis H. F. and Seckler, Henrique S. and Doubleday, Peter F. and Schachner, Luis F. and Srzentić, Kristina and Kelleher, Neil L. and Compton, Philip D.},
month = jan,
year = {2018},
pages = {36--41}
}
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