期刊
MASS SPECTROMETRY REVIEWS
卷 22, 期 5, 页码 287-317出版社
WILEY
DOI: 10.1002/mas.10057
关键词
nucleolar proteins; nucleolin; human parvulin; proteomics; preribosomal ribonucleoprotein complex; electrospray; ionization; time-of-flight mass spectrometry; 2-dimensional; LC-MS/MS analysis; direct nano-LC-MS/MS analysis; dynamome
类别
Proteomic technologies powered by advancements in mass spectrometry and bioinformatics and coupled with accumulated genome sequence data allow a comprehensive study of cell function through large-scale and systematic protein identifications of protein constituents of the cell and tissues, as well as of multi-protein complexes that carry out many cellular function in a higher-order network in the cell. One of the most extensively analyzed cellular functions by proteomics is the production of ribosome, the protein-synthesis machinery, in the nucle(ol)us-the main site of ribosome biogenesis. The use of tagged proteins as affinity bait, coupled with mass spectrometric identification, enabled us to isolate synthetic intermediates of ribosomes that might represent snapshots of nascent ribosomes at particular stages of ribosome biogenesis and to identify their constituents-some of which showed dynamic changes for association with the intermediates at various stages of ribosome biogenesis. In this review, in conjunction with the results from yeast cells, our proteomic approach to analyze ribosome biogenesis in mammalian cells is described. (C) 2003 Wiley Periodicals, Inc.
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