In Vitro Techniques for ADP-Ribosylated Substrate Identification
作者： Giovanna Grimaldi , Giuliana Catara , Carmen Valente , Daniela Corda
DOI: 10.1007/978-1-4939-8588-3_3
关键词:
摘要: ADP-ribosylation is a post-translational modification of proteins that has required the development specific technical approaches for full definition its physiological roles and regulation. The identification enzymes substrates this reaction an instrumental step toward these aims. Here we describe method separation ADP-ribosylated based on use ADP-ribose-binding macro domain thermophilic protein Af1521, coupled to mass spectrometry analysis identification. This foresees coupling resin, affinity-based pull-down assay, specificity resulting from clearing cell lysates with mutated unable bind ADP-ribose. By both mono- poly-ADP-ribosylated have been identified.
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sci-hub.se 参考文章(25)
Daniela Corda, Maria Di Girolamo, Functional aspects of protein mono‐ADP‐ribosylation The EMBO Journal. ,vol. 22, pp. 1953- 1958 ,(2003) , 10.1093/EMBOJ/CDG209
Hisae Kawamitsu, Hiroo Hoshino, Hidechika Okada, Masanao Miwa, Hironao Momoi, Takashi Sugimura, Monoclonal antibodies to poly(adenosine diphosphate ribose) recognize different structures. Biochemistry. ,vol. 23, pp. 3771- 3777 ,(1984) , 10.1021/BI00311A032
Gytis Jankevicius, Markus Hassler, Barbara Golia, Vladimir Rybin, Martin Zacharias, Gyula Timinszky, Andreas G Ladurner, A family of macrodomain proteins reverses cellular mono-ADP-ribosylation Nature Structural & Molecular Biology. ,vol. 20, pp. 508- 514 ,(2013) , 10.1038/NSMB.2523
Ole N. Jensen, Interpreting the protein language using proteomics Nature Reviews Molecular Cell Biology. ,vol. 7, pp. 391- 403 ,(2006) , 10.1038/NRM1939
N. Dani, A. Stilla, A. Marchegiani, A. Tamburro, S. Till, A. G. Ladurner, D. Corda, M. Di Girolamo, Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 106, pp. 4243- 4248 ,(2009) , 10.1073/PNAS.0900066106
Stephanie Jungmichel, Florian Rosenthal, Matthias Altmeyer, Jiri Lukas, Michael O. Hottiger, Michael L. Nielsen, Proteome-wide Identification of Poly(ADP-Ribosyl)ation Targets in Different Genotoxic Stress Responses Molecular Cell. ,vol. 52, pp. 272- 285 ,(2013) , 10.1016/J.MOLCEL.2013.08.026
Thomas MEYER, Helmuth HILZ, Production of anti‐(ADP‐ribose) antibodies with the aid of a dinucleotide‐pyrophosphatase‐resistant hapten and their application for the detection of mono(ADP‐ribosyl)ated polypeptides FEBS Journal. ,vol. 155, pp. 157- 165 ,(1986) , 10.1111/J.1432-1033.1986.TB09471.X
Gyula Timinszky, Susanne Till, Paul O Hassa, Michael Hothorn, Georg Kustatscher, Bianca Nijmeijer, Julien Colombelli, Matthias Altmeyer, Ernst H K Stelzer, Klaus Scheffzek, Michael O Hottiger, Andreas G Ladurner, A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation. Nature Structural & Molecular Biology. ,vol. 16, pp. 923- 929 ,(2009) , 10.1038/NSMB.1664
Florian Rosenthal, Karla L H Feijs, Emilie Frugier, Mario Bonalli, Alexandra H Forst, Ralph Imhof, Hans C Winkler, David Fischer, Amedeo Caflisch, Paul O Hassa, Bernhard Lüscher, Michael O Hottiger, Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases. Nature Structural & Molecular Biology. ,vol. 20, pp. 502- 507 ,(2013) , 10.1038/NSMB.2521
B. Eide, P. Gierschik, A. Spiegel, Immunochemical detection of guanine nucleotide binding proteins mono-ADP-ribosylated by bacterial toxins. Biochemistry. ,vol. 25, pp. 6711- 6715 ,(1986) , 10.1021/BI00369A058