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| Thesis Name： |
Mass spectrometry: A tool for proteomics. |
| Usage： |
chemistry |
| Keyword： |
Mass spectrometry |
| Remarks： |
Proteome has been defined as the PROTEin complement expressed by a genOME ortissue. Proteomics is the field that involves the identification, characterization, andquantification of proteins in tissues or whole cells. In an ideal situation, proteincharacterization would likely include sequence analysis and cellular localization, plusidentification of post-translational modifications, splice variants, and binding partners. In recentyears, mass spectrometric methods have become an essential tool for proteomics research.; In thefirst project, proteins involved in yeast 66S ribosome assembly intermediates were identified from acomplex mixture using nano-flow HPLC (nHPLC) microelectrospray ionization (μESI) massspectrometry. 66S particles were affinity purified and digested with trypsin and the resultingpeptide mixture was analyzed by nHPLC/μESI/MS/MS. A total of 115 proteins were identified. Therole of some of these proteins was examined by determining their subcellular location and byassaying the effects of depleting these proteins on production of 60S subunits.; The second projectinvolved identification of cargoes of nuclear import factors (Karyopherins, or Kaps) and the Kapsthat import histories. The binding partners of 5 Kaps were affinity purified and digested withtrypsin. The resulting peptide mixture was analyzed by mass spectrometry. The Kaps that importhistories H2A, H2B, H3 and H4 were purified in the same manner as above, analyzed by massspectrometry and confirmed by biological techniques. The post-translational modifications of H3 andH4 in the cytosol were characterized by mass spectrometry and the effects of these modifications onthe nuclear localization of H3 and H4 were studied.; The phosphoproteome analysis ofArabidopsis thaliana was reported in the third project. In Arabidopsisthaliana , there is evidence that phosphorylation plays an important role in signaltransduction cascades. However, signal pathways are not known and not much work has been done at theprotein level to identify the substrates of these protein kinases. In this work, total proteinextract of Arabidopsis thaliana was digested with trypsin. The phosphopeptideswere enriched by immobilized metal affinity chromatography (IMAC) and analyzed by mass spectrometry.About 740 phosphopeptides were detected. Sequences for 78 peptides have been confirmed to date.
Author: Guo, Yurong.
Unit: University of Virginia.
ISBN: 0493839305 |
| Original file： |
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