The yeast nucleoporin rip1p contributes to multiple export pathways with no essential role for its FG-repeat region.
The yeast nucleoporin rip1p contributes to multiple export pathways with no essential role for its FG-repeat region.
复制标题
酵母核孔蛋白 rip1p 有助于多种输出途径,但其 FG 重复区域没有重要作用。
DOI:
--
复制
发表时间:
1997
影响因子:
10.5
通讯作者:
Michael Rosbash
中科院分区:
文献类型:
--
作者:
Françoise Stutz;Julia Kantor;Dong Zhang;Terri McCarthy;Megan Neville;Michael Rosbash
The FG-repeat domain of the yeast Rip1 protein (Rip1p) was identified initially as a possible target for the nuclear export signal (NES) of the HIV-1 Rev protein in a yeast two-hybrid assay. Rip1p is inessential, associated with nuclear pore complexes, and structurally related to the FG-nucleoporin family of pore proteins. It contributes to HIV-1 Rev-mediated RNA export and is also important for the export of heat shock RNAs at 42 degrees C. We show here that Rip1p is essential for the export of heat shock RNAs, and this function is fulfilled by the unique carboxyl terminus of Rip1p with no substantial contribution from the FG-repeat region. Genetic interactions between Rip1p and the RNA export mediator Gle1p are described, which support a role of the carboxyl terminus of Rip1p in poly(A)+ RNA export. Finally, this domain of Rip1p also contributes to Rev-mediated RNA export. The data suggest that Rip1p promotes the nuclear export of different classes of substrates by contributing to optimal pore function.
DOI:
10.1073/pnas.87.17.6629
发表时间:
1990
影响因子:
11.1
作者:
Kranz,JE;Holm,C
通讯作者:
Holm,C
影响因子:
10.5
作者:
Saavedra, C;Tung, KS;Cole, CN
通讯作者:
Cole, CN