PXD005542 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The papain-like cysteine proteinases NbCysP6 and NbCysP7 are highly processive enzymes with substrate specificities complementary to Nicotiana benthamiana cathepsin B |
Description | The tobacco-related plant Nicotiana benthamiana is gaining interest as a versatile host for the production of monoclonal antibodies and other protein therapeutics. However, the susceptibility of plant-derived recombinant proteins to endogenous proteolytic enzymes limits their use as biopharmaceuticals. We have now identified two previously uncharacterized N. benthamiana proteases with high antibody-degrading activity, the papain-like cysteine proteinases NbCysP6 and NbCysP7. Both enzymes are capable of hydrolysing a wide range of synthetic substrates, although only NbCysP6 tolerates basic amino acids in its specificity-determining S2 subsite. The overlapping substrate specificities of NbCysP6 and NbCysP7 are also documented by the closely related properties of their other subsites as deduced from the action of the enzymes on proteome-derived peptide libraries. Notable differences were observed to the substrate preferences of N. benthamiana cathepsin B, another antibody-degrading papain-like cysteine proteinase. The complementary activities of NbCysP6, NbCysP7 and N. benthamiana cathepsin B indicate synergistic roles of these proteases in the turnover of recombinant and endogenous proteins in planta, thus representing a paradigm for the shaping of plant proteomes by the combined action of papain-like cysteine proteinases. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-07 |
AnnouncementXML | Submission_2024-10-07_10:06:15.106.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Oliver Schilling |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | dimethylated residue; iodoacetamide derivatized residue |
Instrument | QSTAR; Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-12-12 00:23:56 | ID requested | |
⏵ 1 | 2024-10-07 10:06:15 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Biological |
submitter keyword: Protease, specificity, proteome-derived peptide library |
Contact List
Oliver Schilling |
contact affiliation | Institute of Molecular Medicine and Cell Research University of Freiburg Stefan-Meier-Str. 17, Room 02 027 D-79104 Freiburg, Germany +49 761 203 9615 |
contact email | oliver.schilling@mol-med.uni-freiburg.de |
lab head | |
Oliver Schilling |
contact affiliation | University of Freiburg |
contact email | oliver.schilling@mol-med.uni-freiburg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD005542
- Label: PRIDE project
- Name: The papain-like cysteine proteinases NbCysP6 and NbCysP7 are highly processive enzymes with substrate specificities complementary to Nicotiana benthamiana cathepsin B