The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity
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 ha...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Journal article |
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Elsevier
2016
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| _version_ | 1797072858983170048 |
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| author | Paireder, M Mehofer, U Tholen, S Porodko, A Schähs, P Maresch, D Biniossek, M van der Hoorn, R Lenarcic, B Novinec, M Schilling, O Mach, L |
| author_facet | Paireder, M Mehofer, U Tholen, S Porodko, A Schähs, P Maresch, D Biniossek, M van der Hoorn, R Lenarcic, B Novinec, M Schilling, O Mach, L |
| author_sort | Paireder, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T23:13:44Z |
| format | Journal article |
| id | oxford-uuid:6663eed7-2f61-4a5c-81cb-c48501b185e3 |
| institution | University of Oxford |
| last_indexed | 2024-03-06T23:13:44Z |
| publishDate | 2016 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:6663eed7-2f61-4a5c-81cb-c48501b185e32022-03-26T18:31:36ZThe death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivityJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6663eed7-2f61-4a5c-81cb-c48501b185e3Symplectic Elements at OxfordElsevier2016Paireder, MMehofer, UTholen, SPorodko, ASchähs, PMaresch, DBiniossek, Mvan der Hoorn, RLenarcic, BNovinec, MSchilling, OMach, LThe 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. |
| spellingShingle | Paireder, M Mehofer, U Tholen, S Porodko, A Schähs, P Maresch, D Biniossek, M van der Hoorn, R Lenarcic, B Novinec, M Schilling, O Mach, L The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity |
| title | The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity |
| title_full | The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity |
| title_fullStr | The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity |
| title_full_unstemmed | The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity |
| title_short | The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity |
| title_sort | death enzyme cp14 is a unique papain like cysteine proteinase with a pronounced s2 subsite selectivity |
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