Heat Shock Induced Change in Protein Ubiquitination in Chlamydomonas
スポンサーリンク
概要
- 論文の詳細を見る
Ubiquitin was purified from pea (Pisum sativum L.) and its antibody was produced. Western blot analysis showed that the antibody cross-reacted with ubiquitins from a green alga Chlamydomonas reinhardtii, a brown alga Laminaria angustata and a red alga Porphyridium cruentum but not with ubiquitin from a blue-green alga Synechococcus sp. In Chlamydomonas, the antibody also reacted with some ubiquitinated proteins including 28- and 31-kDa polypeptide. The isoelectric points of Chlamydomonas ubiquitin and the 28- and 31-kDa ubiquitinated proteins were 8.0, 8.9 and 10.3, respectively. The ubiquitinated proteins, including the 28- and 31-kDa polypeptides were detected after in vitro ATP-dependent ubiquitination of Chlamydomonas cell extract with ^<125>I-labeled bovine ubiquitin. Heat treatment of Chlamydomonas cells (>40℃) caused drastic increase of ubiquitinated proteins with high mol wt (>60 kDa), and coordinated redistribution or decrease of other ubiquitinated proteins and free ubiquitin. Quantitative analysis revealed that the 28- and 31-kDa ubiquitinated proteins showed different responses against heat stress, i.e. the former being more sensitive than the latter.
- 日本植物生理学会の論文
著者
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Muto Shoshi
Institute Of Applied Microbiology University Of Tokyo
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Muto Shoshi
Institute Applied Microbiology University Of Tokyo
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Shimogawara K
Teikyo Univ. School Of Medicine Tokyo Jpn
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Shimogawara Kousuke
Institute of Applied Microbiology, University of Tokyo
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