TY - JOUR
T1 - Dataset on interactors of the Arabidopsis thaliana Plant Natriuretic Peptide (AtPNP-A) determined by mass spectrometry
AU - Turek, Ilona
AU - Irving, Helen
AU - Gehring, Christoph A
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: Funding was provided by Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology. We kindly acknowledge KAUST Bioscience Core Laboratory and Dr. Harinda Rajapaksha from La Trobe University Comprehensive Proteomics Platform for assistance with data acquisition and data files conversion, respectively.
PY - 2020/4/22
Y1 - 2020/4/22
N2 - Interactors of the plant natriuretic peptide present in Arabidopsis thaliana, termed AtPNP-A, were affinity-based isolated from A. thaliana (Col-0) leaf mesophyll cell protoplasts by incubating the protoplasts with biologically active biotinylated peptide corresponding to amino acid sequence of the active site of AtPNP-A (pAtPNP-A), either in the presence or absence of a cross-linking agent, 3,3′-dithiobis(sulfosuccinimidyl propionate) (DTSSP), or with equimolar amount of biotin with DTSSP (negative control). Upon biotin/streptavidin-based isolation of proteins bound to the pAtPNP-A or biotin, the proteins were separated by sodium dodecyl sulphate – polyacrylamide gel electrophoresis (SDS-PAGE), digested with trypsin and subjected to identification with liquid chromatography tandem mass spectrometry (LC-MS/MS). Label-free quantification of identified proteins allowed identification of binding partners of AtPNP-A, paving the way for pinpointing novel signal transduction pathways AtPNP-A is involved in. The raw and processed LC-MS/MS data reported in this article have been deposited to the ProteomeXchange Consortium with the dataset identifier PXD017925.
AB - Interactors of the plant natriuretic peptide present in Arabidopsis thaliana, termed AtPNP-A, were affinity-based isolated from A. thaliana (Col-0) leaf mesophyll cell protoplasts by incubating the protoplasts with biologically active biotinylated peptide corresponding to amino acid sequence of the active site of AtPNP-A (pAtPNP-A), either in the presence or absence of a cross-linking agent, 3,3′-dithiobis(sulfosuccinimidyl propionate) (DTSSP), or with equimolar amount of biotin with DTSSP (negative control). Upon biotin/streptavidin-based isolation of proteins bound to the pAtPNP-A or biotin, the proteins were separated by sodium dodecyl sulphate – polyacrylamide gel electrophoresis (SDS-PAGE), digested with trypsin and subjected to identification with liquid chromatography tandem mass spectrometry (LC-MS/MS). Label-free quantification of identified proteins allowed identification of binding partners of AtPNP-A, paving the way for pinpointing novel signal transduction pathways AtPNP-A is involved in. The raw and processed LC-MS/MS data reported in this article have been deposited to the ProteomeXchange Consortium with the dataset identifier PXD017925.
UR - http://hdl.handle.net/10754/662614
UR - https://linkinghub.elsevier.com/retrieve/pii/S235234092030500X
UR - http://www.scopus.com/inward/record.url?scp=85084141547&partnerID=8YFLogxK
U2 - 10.1016/j.dib.2020.105606
DO - 10.1016/j.dib.2020.105606
M3 - Article
C2 - 32395580
SN - 2352-3409
VL - 30
SP - 105606
JO - Data in Brief
JF - Data in Brief
ER -