Stage-specific changes in protein synthesis during conjugation in Tetrahymena thermophila.

Stage-specific changes in protein synthesis during conjugation in Tetrahymena thermophila.
复制标题

嗜热四膜虫接合过程中蛋白质合成的阶段特异性变化。

DOI:
10.1016/0014-4827(84)90388-4
复制
发表时间:
1984
影响因子:
3.7
通讯作者:
P. Suhr
P. Suhr
中科院分区:
医学3区
文献类型:
--
作者:
P. Suhr

文献摘要

被引文献

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嗜热四膜虫(Tetrahymena thermophilais)是一种可诱导的发育系统,它能导致一对中两个配偶体的遗传物质同步重组。随后的细胞学事件,同时交配细胞和蛋白质合成的Feulgen染色显示使用[35S]蛋氨酸脉冲标记和二维凝胶电泳。至少有33个蛋白质,包括24个结合特异性蛋白质,其表观分子量(Mr)在61至200 × 103之间。两种微酸性蛋白(分别为Mr89和73 × 103)在交配感受态细胞混合后不久,主要在紧密配对形成之前受到刺激。在减数分裂过程中,有10种蛋白质受到刺激,其中两种(Mr90和78 × 103)特别有趣,因为它们受到高度刺激,比大多数其他检测到的蛋白质更具碱性(pI值约为8.5)。12个蛋白质刺激基本上配对和早期大核发育之间,三个被刺激前不久合子形成和在postzygotic分裂,和6个被刺激在后期接合,在大核发育的各个部分。结合刺激蛋白的功能进行了讨论。
Conjugation in the free-living ciliateTetrahymena thermophilais an inducible developmental system which results in a synchronized reorganization of the genetic material in both mates of a pair. The cytological events were followed by Feulgen stainings of simultaneously mating cells and protein synthesis was revealed using [35S]methionine pulse labelling and two-dimensional gel electrophoresis. At least 33 proteins, including 24 conjugation-specific proteins, with apparent molecular weights (Mr) between 61 and 200 × 103are stimulated during conjugation. Two slightly acidic proteins (Mr89 and 73 × 103, respectively) are stimulated shortly after mixing of mating-competent cells and mainly before tight pairs are formed. Ten proteins are stimulated during meiosis, and two of these (Mr90 and 78 × 103, respectively) are particularly interesting, since they are highly stimulated and more basic (pI values around 8.5) than most other proteins detected. Twelve proteins are stimulated essentially between pairing and early macronuclear development, three are stimulated from shortly before zygote formation and during the postzygotic divisions, and six are stimulated during late conjugation, at various parts of macronuclear development. The functions of the conjugation-stimulated proteins are discussed.