The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity

Abstract: The cysteine protease CP14 has been identified as a central component of a molecular module regulating programmed cell death in plant embryos. CP14 belongs to a distinct subfamily of papain-like cysteine proteinases of which no representative has been characterized thoroughly to date. However, it has been proposed that CP14 is a cathepsin H-like protease. We have now produced recombinant Nicotiana benthamiana CP14 (NbCP14) lacking the C-terminal granulin domain. As typical for papain-like cysteine proteinases, NbCP14 undergoes rapid autocatalytic activation when incubated at low pH. The mature protease is capable of hydrolysing several synthetic endopeptidase substrates, but cathepsin H-like aminopeptidase activity could not be detected. NbCP14 displays a strong preference for aliphatic over aromatic amino acids in the specificity-determining P2 position. This subsite selectivity was also observed upon digestion of proteome-derived peptide libraries. Notably, the specificity profile of NbCP14 differs from that of aleurain-like protease, the N. benthamiana orthologue of cathepsin H. We conclude that CP14 is a papain-like cysteine proteinase with unusual enzymatic properties which may prove of central importance for the execution of programmed cell death during plant development

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• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch
• Notes: Archives of biochemistry and biophysics. - 603 (2016) , 110-117, ISSN: 0003-9861

Contributors, Places and Time

• Event: Veröffentlichung
• (where): Freiburg
• (who): Universität
• (when): 2025
• Creator: Paireder, Melanie ; Mehofer, Ulrich ; Tholen, Stefan ; Porodko, Andreas ; Schähs, Philipp ; Maresch, Daniel ; Biniossek, Martin Lothar ; Hoorn, Renier A. L. van der ; Lenarcic, Brigita ; Novinec, Marko ; Schilling, Oliver ; Mach, Lukas
• Contributor: Zentrum für Biochemie und Molekulare Zellforschung

Further information

• DOI: 10.1016/j.abb.2016.05.017
• URN: urn:nbn:de:bsz:25-freidok-1317986
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.