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首页> 外文期刊>Molecular and Cellular Biology >Interactions among Drosophila Nuclear Envelope Proteins Lamin, Otefin, and YA
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Interactions among Drosophila Nuclear Envelope Proteins Lamin, Otefin, and YA

机译：果蝇核包膜蛋白Lamin，Otefin和YA之间的相互作用

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The nuclear envelope plays many roles, including organizing nuclear structure and regulating nuclear events. Molecular associations of nuclear envelope proteins may contribute to the implementation of these functions. Lamin, otefin, and YA are the three Drosophilanuclear envelope proteins known in early embryos. We used the yeast two-hybrid system to explore the interactions between pairs of these proteins. The ubiquitous major lamina protein, lamin Dm, interacts with both otefin, a peripheral protein of the inner nuclear membrane, and YA, an essential, developmentally regulated protein of the nuclear lamina. In agreement with this interaction, lamin and otefin can be coimmunoprecipitated from the vesicle fraction ofDrosophila embryos and colocalize in nuclear envelopes ofDrosophila larval salivary gland nuclei. The two-hybrid system was further used to map the domains of interaction among lamin, otefin, and YA. Lamin’s rod domain interacts with the complete otefin protein, with otefin’s hydrophilic NH2-terminal domain, and with two different fragments derived from this domain. Analogous probing of the interaction between lamin and YA showed that the lamin rod and tail plus part of its head domain are needed for interaction with full-length YA in the two-hybrid system. YA’s COOH-terminal region is necessary and sufficient for interaction with lamin. Our results suggest that interactions with lamin might mediate or stabilize the localization of otefin and YA in the nuclear lamina. They also suggest that the need for both otefin and lamin in mediating association of vesicles with chromatin might reflect the function of a protein complex that includes these two proteins.
机译：核包裹层起着许多作用，包括组织核结构和调节核事件。核被膜蛋白的分子缔合可能有助于实现这些功能。 Lamin，otefin和YA是果蝇早期胚胎中已知的三种果蝇核包膜蛋白。我们使用酵母双杂交系统来探索这些蛋白质对之间的相互作用。普遍存在的主要椎板蛋白lamin Dm与otefin（内核膜的外围蛋白）和YA（一种必需的，发育受调控的核板蛋白）相互作用。与这种相互作用相一致，可以从果蝇胚胎的囊泡组分中共沉淀免疫沉淀沉淀的lamin和otefin，并将它们共定位在果蝇幼虫唾液腺核的核膜中。两杂化系统进一步用于绘制层粘蛋白，奥特芬和YA之间相互作用的区域。 Lamin的杆状结构域与完整的otefin蛋白，otefin的亲水性NH 2 末端结构域以及与该结构域衍生的两个不同片段发生相互作用。对lamin和YA之间相互作用的类似探测表明，lamin杆和尾巴以及其头部的一部分与两杂交系统中的全长YA相互作用是必需的。 YA的COOH末端区域对于与lamin相互作用是必要和充分的。我们的结果表明，与核纤层蛋白的相互作用可能介导或稳定了otefin和YA在核层中的定位。他们还暗示，在介导囊泡与染色质缔合过程中，对otefin和lamin的需求都可能反映了包含这两种蛋白质的蛋白质复合物的功能。

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