XB-ART-41551Dev Biol August 1, 2010; 344 (1): 272-83.
The translational regulation of maternal mRNAs is one of the most important steps in the control of temporal-spatial gene expression during oocyte maturation and early embryogenesis in various species. Recently, it has become clear that protein components of mRNPs play essential roles in the translational regulation of maternal mRNAs. In the present study, we investigated the function of P100 in Xenopus oocytes. P100 exhibits sequence conservation with budding yeast Pat1 and is likely the orthologue of human Pat1a (also called PatL2). P100 is maternally expressed in immature oocytes, but disappears during oocyte maturation. In oocytes, P100 is an RNA binding component of ribosome-free mRNPs, associating with other mRNP components such as Xp54, xRAP55 and CPEB. Translational repression by overexpression of P100 occurred when reporter mRNAs were injected into oocytes. Intriguingly, we found that when P100 was overexpressed in the oocytes, the kinetics of oocyte maturation was considerably retarded. In addition, overexpression of P100 in oocytes significantly affected the accumulation of c-Mos and cyclin B1 during oocyte maturation. These results suggest that P100 plays a role in regulating the translation of specific maternal mRNAs required for the progression of Xenopus oocyte maturation.
PubMed ID: 20471969
Article link: Dev Biol
Species referenced: Xenopus
Genes referenced: ccnb1.2 cpeb1 ddx6 hbg1 lsm1 lsm14a mos patl1 patl2 set spdyc ybx2
Antibodies: Actb Ab1 Ccnb1 Ab1 Cpeb1 Ab1 Lsm1 Ab1 Lsm14a Ab1 Mapk1 Ab5 Mos Ab1 Set Ab1
Morpholinos: patl2 MO1
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