Bon E, Recordon-Navarro P, Durrens P, Iwase M, Toh-E A, Aigle M
Laboratoire de Biologie Cellulaire de la Levure, IBGC, 1 rue Camille Saint-Saëns, 33077 Bordeaux, France.
Yeast. 2000 Sep 30;16(13):1229-41. doi: 10.1002/1097-0061(20000930)16:13<1229::AID-YEA618>3.0.CO;2-Q.
The Rvs161p and Rvs167p proteins of Saccharomyces cerevisiae, homologues of higher eukaryotes' amphiphysins, associate with actin and appear to be involved in several functions related to the actin cytoskeleton. In order to identify partners of the Rvsp proteins, yeast libraries constructed in two-hybrid vectors were screened using either Rvs167p or Rvs161p as a bait. The selected candidates, representing 34 ORFs, were then tested against both Rvsp proteins, as well as domains of Rvs167p or Rvs161p. Among the most significant ones, 24 ORFs were specific preys of Rvs167p only and two gave interactions with Rvs161p only. Interestingly, five ORFs were preys of both Rvs161p and Rvs167p (RVS167, LAS17, YNL094w, YMR192w and YPL249c). Analysis of putative functions of the candidates confirm involvement of the Rvsp in endocytosis/vesicle traffic, but also opens possible new fields, such as nuclear functions.
酿酒酵母的Rvs161p和Rvs167p蛋白是高等真核生物发动蛋白的同源物，它们与肌动蛋白相关，并且似乎参与了与肌动蛋白细胞骨架相关的多种功能。为了鉴定Rvsp蛋白的相互作用蛋白，使用Rvs167p或Rvs161p作为诱饵筛选了构建在双杂交载体中的酵母文库。然后针对两种Rvsp蛋白以及Rvs167p或Rvs161p的结构域对所选的代表34个开放阅读框的候选蛋白进行了测试。在最显著的候选蛋白中，24个开放阅读框仅是Rvs167p的特异性猎物，两个仅与Rvs161p有相互作用。有趣的是，五个开放阅读框是Rvs161p和Rvs167p两者的猎物（RVS167、LAS17、YNL094w、YMR192w和YPL249c）。对候选蛋白推定功能的分析证实Rvsp参与了内吞作用/囊泡运输，但也开辟了可能的新领域，如核功能。
