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甜菜黄化脉明病毒的HSP70相关65 kDa蛋白是一种微管结合蛋白。

HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein.

作者信息

Karasev A V, Kashina A S, Gelfand V I, Dolja V V

机构信息

Institute of Microbiology, Academy of Sciences of Russia, Moscow.

出版信息

FEBS Lett. 1992 Jun 8;304(1):12-4. doi: 10.1016/0014-5793(92)80578-5.

Abstract

Beet yellows virus (BYV) genome encodes a 65 kDa protein homologous to the HSP70 family of cellular heat-shock proteins (Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V. and Dolja, V.V. (1991) J. Mol. Biol. 217, 603-610). The respective gene was cloned and expressed in vitro yielding a product of the expected size (p65). This product was found to bind to the purified microtubules with a binding constant of 4 x 10(-7) M. The binding of p65 was stimulated if ATP presented in the translation mixture was hydrolyzed by apyrase. Removal of the short C-terminal domains of alpha- and beta-tubulin by subtilisin digestion abolished the binding, demonstrating its specificity. The possible role of p65 association with microtubules in the movement of virus within and/or between plant cells is proposed.

摘要

甜菜黄化病毒(BYV)基因组编码一种65 kDa的蛋白质,该蛋白质与细胞热休克蛋白的HSP70家族同源(阿格拉诺夫斯基,A.A.,博伊科,V.P.,卡拉塞夫,A.V.,库宁,E.V.和多尔贾,V.V.(1991年)《分子生物学杂志》217卷,603 - 610页)。相应的基因被克隆并在体外表达,产生预期大小的产物(p65)。发现该产物以4×10⁻⁷ M的结合常数与纯化的微管结合。如果翻译混合物中存在的ATP被硫酸腺苷酶水解,p65的结合会受到刺激。通过枯草杆菌蛋白酶消化去除α-和β-微管蛋白的短C末端结构域可消除这种结合,证明了其特异性。文中提出了p65与微管结合在病毒在植物细胞内和/或细胞间移动中的可能作用。

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