N‐ and C‐terminal degradomics: new approaches to reveal biological roles for plant proteases from substrate identification

作者: Pitter F. Huesgen , Christopher M. Overall

DOI: 10.1111/J.1399-3054.2011.01536.X

关键词:

摘要: Proteolysis is an irreversible post-translational modification that regulates many intra- and intercellular processes, including essential go/no-go decisions during cell proliferation, development death. Hundreds of protease-coding genes have been identified in plants, but few linked to specific substrates. Conversely, proteolytic processes are frequently observed plant biology rarely they ascribed proteases. In mammalian systems, unbiased system-wide proteomics analyses protease activities recently tremendously successful the identification substrate repertoires, also known as degradomes. Knowledge degradome key understand role proteases vivo. Quantitative shotgun proteomic studies identifying substrates, while simple perform biased toward abundant proteins do not reveal precise cleavage sites. Current degradomics techniques overcome these limitations by focusing on information-rich amino- carboxy-terminal peptides original mature protease-generated neo-termini. Targeted quantitative analysis protein termini identifies sites substrates with exquisite sensitivity dynamic range vitro vivo systems. This review provides overview state-of-the-art methods for enrichment terminal peptides, their application research. These emerging promise clarify elusive biological roles proteolysis plants.

参考文章(43)
Oliver Schilling, Pitter F. Huesgen, Olivier Barré, Christopher M. Overall, Identification and relative quantification of native and proteolytically generated protein C-termini from complex proteomes: C-terminome analysis. Methods of Molecular Biology. ,vol. 781, pp. 59- 69 ,(2011) , 10.1007/978-1-61779-276-2_4
Petra Van Damme, Francis Impens, Joël Vandekerckhove, Kris Gevaert, Protein processing characterized by a gel-free proteomics approach. Methods of Molecular Biology. ,vol. 484, pp. 245- 262 ,(2008) , 10.1007/978-1-59745-398-1_16
An Staes, Petra Van Damme, Kenny Helsens, Hans Demol, Joël Vandekerckhove, Kris Gevaert, Improved recovery of proteome-informative, protein N-terminal peptides by combined fractional diagonal chromatography (COFRADIC). Proteomics. ,vol. 8, pp. 1362- 1370 ,(2008) , 10.1002/PMIC.200700950
Mari Enoksson, Jingwei Li, Melanie M. Ivancic, John C. Timmer, Eric Wildfang, Alexey Eroshkin, Guy S. Salvesen, W. Andy Tao, Identification of proteolytic cleavage sites by quantitative proteomics. Journal of Proteome Research. ,vol. 6, pp. 2850- 2858 ,(2007) , 10.1021/PR0701052
Francis Impens, Niklaas Colaert, Kenny Helsens, Kim Plasman, Petra Van Damme, Joël Vandekerckhove, Kris Gevaert, MS-driven protease substrate degradomics. Proteomics. ,vol. 10, pp. 1284- 1296 ,(2010) , 10.1002/PMIC.200900418
T. K. Chang, D. Y. Jackson, J. P. Burnier, J. A. Wells, Subtiligase: a tool for semisynthesis of proteins Proceedings of the National Academy of Sciences of the United States of America. ,vol. 91, pp. 12544- 12548 ,(1994) , 10.1073/PNAS.91.26.12544
Kris Gevaert, Petra Van Damme, Bart Ghesquière, Francis Impens, Lennart Martens, Kenny Helsens, Joël Vandekerckhove, A la carte proteomics with an emphasis on gel-free techniques. Proteomics. ,vol. 7, pp. 2698- 2718 ,(2007) , 10.1002/PMIC.200700114
G. Xu, S. B. Y. Shin, S. R. Jaffrey, Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini Proceedings of the National Academy of Sciences of the United States of America. ,vol. 106, pp. 19310- 19315 ,(2009) , 10.1073/PNAS.0908958106
Oliver Schilling, Pitter F Huesgen, Olivier Barré, Ulrich auf dem Keller, Christopher M Overall, Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry Nature Protocols. ,vol. 6, pp. 111- 120 ,(2011) , 10.1038/NPROT.2010.178