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Journal of Cell Science, Vol 111, Issue 13 1889-1896, Copyright © 1998 by Company of Biologists

JOURNAL ARTICLES

The nuclear import factor p10 regulates the functional size of the nuclear pore complex during oogenesis

C Feldherr, D Akin and MS Moore
Dept of Anatomy and Cell Biology, University of Florida, College of Medicine, Gainesville, FL 32610, USA. feldherr@college.med.ufl.edu

Previtellogenic, stage-1 Xenopus oocytes produce mainly 5S and tRNA, whereas vitellogenic oocytes, stages 2-6, synthesize predominantly 18S and 28S rRNA. Using nucleoplasmin-coated gold as a transport substrate, it was determined that the shift in synthesis from small to large RNAs during oogenesis is accompanied by an increase in both the rates of signal-mediated nuclear import and the functional size of nuclear pores. It was observed that, despite the reduction in transport capacity, gold still accumulated at the cytoplasmic surface of the pores in stage-1 oocytes. This suggested that transport in these cells is limited by translocation factors, rather than by cytoplasmic binding factors. Analysis of extracts prepared from stage-1 and vitellogenic oocytes revealed that the transport factor p10 is more abundant in stage-1 cells. Microinjection of purified p10 into stage-2 oocytes reduced the nuclear import of large gold particles to the level observed in stage-1 cells. It is concluded that p10 can modulate transport through the pores by regulating the functional size of the central transporter element.
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