碩士 / 國立陽明大學 / 遺傳學研究所 / 93 / To understand the effect of the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) within protein structure to the nuclear trafficking, the NH2-terminal region of human ribosomal protein L7 was chosen as the study model, because the NH2 terminus of L7 is capable of entering the nucleus and the nucleolus. The NH2 terminus can be divided into four motifs, N1, N2, N3 and N4, according to the knowledge of the SV 40 T antigen NLS. Each motif was separately fused to the NH2 terminus of 3 copies of enhanced green fluorescence protein ((EGFP)3) to investigate their NLS ability. These constructs were transfected into HeLa cell. The localization of transiently expressed proteins in cells were observed using confocal microscope. Among these motifs, N2, N3 and N4, but not N1, function as NLSs, however, none of them can make (EGFP)3 entering the nucleoli. By making combinations of different motifs with (EGFP)3, the nucleolus entry was examined. The results found that (EGFP)3 get into the nucleolus only when the entire sequence of N1, N2, N3 and N4 exist.
| Identifer | oai:union.ndltd.org:TW/093YM005498013 |
| Date | January 2005 |
| Creators | I-fang Lee, 李逸芳 |
| Contributors | Alan Lin, 林茂榮 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 54 |
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