PXD046396 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Mass spectrometry distinguishes putrescine, spermidine, and spermine covalently attached to proteins |
Description | Bacterial and mammalian cells are rich in putrescine, spermidine and spermine. Polyamines can be incorporated into proteins in vitro. Very few naturally occurring polyaminated proteins have been identified. Bovine albumin and the recombinant universal stress protein from Francisella tularensis were used as models for mass spectrometry analysis of polyaminated proteins. The proteins were covalently bound to putrescine, spermidine, or spermine by the action of carbodiimide or microbial transglutaminase. Tryptic peptides were subjected to liquid chromatography tandem mass spectrometry. Adducts were identified by Protein Prospector software. We describe the search parameters for identifying polyaminated peptides in Protein Prospector and show convincing MMS spectra for adducts with putrescine, spermidine, and spermine. Manual evaluation led us to recognize signature ions for polyamine adducts on Asp, Glu, and Gln. Manual evaluation recognized neutral loss from putrescine, spermidine and spermine during the fragmentation process. Mechanisms for formation of signature ions and neutral loss are presented. Manual evaluation recognized a false positive adduct which had been formed during trypsinolysis by rearrangement of a peptide sequence. Another false positive was a 71 Da added mass on cysteine, which was initially assumed to be putrescine, but was actually a propionamide adduct for a sample extracted from a polyacrylamide gel. The type of information presented in this report serves as a model for identifying naturally occurring polyaminated proteins. |
HostingRepository | PRIDE |
AnnounceDate | 2024-02-28 |
AnnouncementXML | Submission_2024-02-28_02:36:53.009.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Lawrence Schopfer |
SpeciesList | scientific name: Bos taurus (Bovine); NCBI TaxID: 9913; |
ModificationList | amidated residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-10-25 11:58:41 | ID requested | |
⏵ 1 | 2024-02-28 02:36:53 | announced | |
Publication List
Schopfer LM, Girardo B, Lockridge O, Larson MA, Universal Stress Protein and Bovine Albumin. Biochem Res Int, 2024():7120208(2024) [pubmed] |
10.1155/2024/7120208; |
Keyword List
submitter keyword: polyamine, universal stress protein, transglutaminase, mass spectrometry, manual evaluation, carbodiimide, albumin |
Contact List
Oksana Lockridge |
contact affiliation | Eppley Institute University of Nebraska Medical Center USA |
contact email | olockrid@unmc.edu |
lab head | |
Lawrence Schopfer |
contact affiliation | University of Nebraska Medical Center |
contact email | lmschopf@unmc.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD046396
- Label: PRIDE project
- Name: Mass spectrometry distinguishes putrescine, spermidine, and spermine covalently attached to proteins