التفاصيل البيبلوغرافية
| العنوان: |
Dual-Stage Neutral Loss Tandem Mass Spectrometric Strategy for Confident Identification of Protein Prenylation |
| المؤلفون: |
Zixiang Fang (6430112), Saiful M. Chowdhury (1654066) |
| سنة النشر: |
2021 |
| المجموعة: |
Smithsonian Institution: Digital Repository |
| مصطلحات موضوعية: |
Biophysics, Biochemistry, Medicine, Genetics, Molecular Biology, Biotechnology, Developmental Biology, Cancer, Inorganic Chemistry, Hematology, Infectious Diseases, Chemical Sciences not elsewhere classified, phase cleavable properties, efficient enrichment technique, abundance farnesyl peptide, rsoh group ), r group ), native prenyl proteins, regulates protein interactions, mouse macrophage cells, 3 , 2 , prenyl thioether bond, prenylation study workflow, prior ms studies, oxidized prenyl group, consistent neutral loss, native protein prenylation, prenyl group, oxidized thioether |
| الوصف: |
Protein prenylation is an important post-translational modification that regulates protein interactions, localizations, and signaling pathways in normal functioning of eukaryotic cells. It is also a critical step in the oncogenic developments of various cancers. Direct identification of native protein prenylation by mass spectrometry (MS) has been challenging due to high hydrophobicity and the lack of an efficient enrichment technique. Prior MS studies of prenylation revealed that prenyl peptides readily generate high-intensity fragments after neutral loss of the prenyl group (R group), and more recent investigation of oxidized prenyl peptides discovered more consistent neutral loss of the oxidized prenyl group (RSOH group). Here, a dual-stage neutral loss MS 3 (DS-NLMS3)-based strategy is therefore developed by combining both gas-phase cleavable properties of the prenyl thioether bond and mono-oxidized thioether to improve the large-scale identification of prenylation. Both neutral losses can individually and distinctively confirm the prenylation type in MS 2 and the sequence of the prenyl peptide upon targeted MS 3 fragmentation. This dual-faceted NLMS3 strategy significantly improves the confidence in the identification of protein prenylation from large-scale samples, which enables the unambiguous identification of prenylated sites of the spiked low-abundance farnesyl peptide and native prenyl proteins from mouse macrophage cells, even without prior enrichment during sample preparation. The ease of incorporating this strategy into the prenylation study workflow and minimum disruption to the biological lipidome are advantageous for unraveling unknown native protein prenylation and further developments in profiling and quantifying prenylome. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
unknown |
| العلاقة: |
https://figshare.com/articles/journal_contribution/Dual-Stage_Neutral_Loss_Tandem_Mass_Spectrometric_Strategy_for_Confident_Identification_of_Protein_Prenylation/16677526Test |
| DOI: |
10.1021/acs.analchem.1c01617.s001 |
| الإتاحة: |
https://doi.org/10.1021/acs.analchem.1c01617.s001Test |
| حقوق: |
CC BY-NC 4.0 |
| رقم الانضمام: |
edsbas.EBF0B594 |
| قاعدة البيانات: |
BASE |
