碩士 / 臺灣大學 / 微生物與生化學研究所 / 98 / The SUMO E3 ligase involves in the last step of sumoylation. In addition to faciliate sumoylation and increase specificity for the targets, SUMO E3 ligases modulate a wide range of physiological functions. There are many sumoylated proteins in the cells, but only three kinds of SUMO E3 ligases have been shown in the literatures. Notably, the study of SUMO E3 ligase in Chlamydomonas reinhardtii has not been reported.
In this study, using the Arabidopsis SUMO E3 ligase, AtSiz1, as the template for BLAST search, a gene encoding for a predicated protein with unkown function has been remarked. This predicated protein has similar conserved domains with AtSiz1, such as N-terminal SAP (scaffold attachment factor A/B/Acinus/PIAS) domain, PHD (plant homeodoamin) and RING (really interesting new gene) domain in the middle of the sequence. Based on the sequence observation, this predicated protein was herein named CrSiz1. The partial sequences of CrSiz1 have been expressed and purified from the Escherichia coli. It is noted that CrSiz1 cotains a unique C-terminal sequence which has not been found in other Siz1 proteins. It has been reported that AtSiz1 can inscrease sumoylated proteins under the heat shock condition. By using the antibodies specific to CrSiz1 for western blotting against the C. reinhardtii samples obtained from the cells cultured at 42
| Identifer | oai:union.ndltd.org:TW/098NTU05381037 |
| Date | January 2010 |
| Creators | Ya-Ling Tseng, 曾雅伶 |
| Contributors | 張世宗 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 77 |
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