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Regulated interaction between polypeptide chain elongation factor-1 complex with the 26S proteasome during <Emphasis Type="Italic">Xenopus</Emphasis> oocyte maturation
Authors:Email author" target="_blank">Toshinobu?TokumotoEmail author  Ayami?Kondo  Junko?Miwa  Ryo?Horiguchi  Mika?Tokumoto  Yoshitaka?Nagahama  Noriyuki?Okida  Katsutoshi?Ishikawa
Institution:(1) Department of Biology and Geosciences, Faculty of Science, Shizuoka University, Shizuoka 422-8529, Japan;(2) CREST Research Project, Japan Science and Technology Corporation, Japan;(3) Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan;(4) Department of Molecular Biomechanics, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan
Abstract:

Background  

During Xenopusoocyte maturation, the amount of a 48 kDa protein detected in the 26S proteasome fraction (p48) decreased markedly during oocyte maturation to the low levels seen in unfertilized eggs. The results indicate that the interaction of at least one protein with the 26S proteasome changes during oocyte maturation and early development. An alteration in proteasome function may be important for the regulation of developmental events, such as the rapid cell cycle, in the early embryo. In this study, we identified p48.
Keywords:
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