Abstract
An3 is a maternal mRNA localized to the animal hemisphere of oocytes and early embryos. We have analyzed the enzymatic activity and the subcellular localization of the protein encoded by An3 mRNA during Xenopus oogenesis. Antibodies raised using recombinant full-length and truncated An3 protein recognized a single protein in Xenopus and single proteins from HeLa cells, Drosophila, mouse testes, and Saccharomyces cerevisiae. An3 protein immunoprecipitated from stage IV and stage VI oocytes had ATP-dependent RNA helicase activity. The subcellular location of An3 protein changed during oocyte development. In previtellogenic oocytes, An3 was present throughout the nucleus; cytoplasmic localization was relatively sparse. Nuclear localization in mid-vitellogenic oocytes was primarily nucleolar; cytoplasmic staining increased relative to earlier stages. In stage VI oocytes, An3 protein was detected only in the cytoplasm. The temporal change in An3 protein localization is consistent with a role in the production of large maternal pools of rRNA during oogenesis.
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Selected References
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- Caizergues-Ferrer M., Mathieu C., Mariottini P., Amalric F., Amaldi F. Developmental expression of fibrillarin and U3 snRNA in Xenopus laevis. Development. 1991 May;112(1):317–326. doi: 10.1242/dev.112.1.317. [DOI] [PubMed] [Google Scholar]
- Dumont J. N. Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals. J Morphol. 1972 Feb;136(2):153–179. doi: 10.1002/jmor.1051360203. [DOI] [PubMed] [Google Scholar]
- Gururajan R., Perry-O'Keefe H., Melton D. A., Weeks D. L. The Xenopus localized messenger RNA An3 may encode an ATP-dependent RNA helicase. Nature. 1991 Feb 21;349(6311):717–719. doi: 10.1038/349717a0. [DOI] [PubMed] [Google Scholar]
- Iggo R. D., Lane D. P. Nuclear protein p68 is an RNA-dependent ATPase. EMBO J. 1989 Jun;8(6):1827–1831. doi: 10.1002/j.1460-2075.1989.tb03577.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jamieson D. J., Rahe B., Pringle J., Beggs J. D. A suppressor of a yeast splicing mutation (prp8-1) encodes a putative ATP-dependent RNA helicase. Nature. 1991 Feb 21;349(6311):715–717. doi: 10.1038/349715a0. [DOI] [PubMed] [Google Scholar]
- Jaramillo M., Dever T. E., Merrick W. C., Sonenberg N. RNA unwinding in translation: assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-4F and eIF-4B. Mol Cell Biol. 1991 Dec;11(12):5992–5997. doi: 10.1128/mcb.11.12.5992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lee C. G., Hurwitz J. Human RNA helicase A is homologous to the maleless protein of Drosophila. J Biol Chem. 1993 Aug 5;268(22):16822–16830. [PubMed] [Google Scholar]
- Linnen J. M., Bailey C. P., Weeks D. L. Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins. Gene. 1993 Jun 30;128(2):181–188. doi: 10.1016/0378-1119(93)90561-g. [DOI] [PubMed] [Google Scholar]
- Mosquera L., Forristall C., Zhou Y., King M. L. A mRNA localized to the vegetal cortex of Xenopus oocytes encodes a protein with a nanos-like zinc finger domain. Development. 1993 Jan;117(1):377–386. doi: 10.1242/dev.117.1.377. [DOI] [PubMed] [Google Scholar]
- Otte A. P., McGrew L. L., Olate J., Nathanson N. M., Moon R. T. Expression and potential functions of G-protein alpha subunits in embryos of Xenopus laevis. Development. 1992 Sep;116(1):141–146. doi: 10.1242/dev.116.1.141. [DOI] [PubMed] [Google Scholar]
- Pause A., Méthot N., Sonenberg N. The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol Cell Biol. 1993 Nov;13(11):6789–6798. doi: 10.1128/mcb.13.11.6789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peng H. B. Xenopus laevis: Practical uses in cell and molecular biology. Solutions and protocols. Methods Cell Biol. 1991;36:657–662. [PubMed] [Google Scholar]
- Ripmaster T. L., Vaughn G. P., Woolford J. L., Jr A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly. Proc Natl Acad Sci U S A. 1992 Dec 1;89(23):11131–11135. doi: 10.1073/pnas.89.23.11131. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenberg A. H., Lade B. N., Chui D. S., Lin S. W., Dunn J. J., Studier F. W. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene. 1987;56(1):125–135. doi: 10.1016/0378-1119(87)90165-x. [DOI] [PubMed] [Google Scholar]
- Sachs A. B., Davis R. W. Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. Science. 1990 Mar 2;247(4946):1077–1079. doi: 10.1126/science.2408148. [DOI] [PubMed] [Google Scholar]
- Schmid S. R., Linder P. D-E-A-D protein family of putative RNA helicases. Mol Microbiol. 1992 Feb;6(3):283–291. doi: 10.1111/j.1365-2958.1992.tb01470.x. [DOI] [PubMed] [Google Scholar]
- Schwartz S. P., Aisenthal L., Elisha Z., Oberman F., Yisraeli J. K. A 69-kDa RNA-binding protein from Xenopus oocytes recognizes a common motif in two vegetally localized maternal mRNAs. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11895–11899. doi: 10.1073/pnas.89.24.11895. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwer B., Guthrie C. PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature. 1991 Feb 7;349(6309):494–499. doi: 10.1038/349494a0. [DOI] [PubMed] [Google Scholar]
- Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
- Smith R. C., Dworkin M. B., Dworkin-Rastl E. Destruction of a translationally controlled mRNA in Xenopus oocytes delays progesterone-induced maturation. Genes Dev. 1988 Oct;2(10):1296–1306. doi: 10.1101/gad.2.10.1296. [DOI] [PubMed] [Google Scholar]
- Thomsen G. H., Melton D. A. Processed Vg1 protein is an axial mesoderm inducer in Xenopus. Cell. 1993 Aug 13;74(3):433–441. doi: 10.1016/0092-8674(93)80045-g. [DOI] [PubMed] [Google Scholar]
- Wassarman D. A., Steitz J. A. RNA splicing. Alive with DEAD proteins. Nature. 1991 Feb 7;349(6309):463–464. doi: 10.1038/349463a0. [DOI] [PubMed] [Google Scholar]
- Weeks D. L., Melton D. A. A maternal mRNA localized to the animal pole of Xenopus eggs encodes a subunit of mitochondrial ATPase. Proc Natl Acad Sci U S A. 1987 May;84(9):2798–2802. doi: 10.1073/pnas.84.9.2798. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weeks D. L., Melton D. A. A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes for a growth factor related to TGF-beta. Cell. 1987 Dec 4;51(5):861–867. doi: 10.1016/0092-8674(87)90109-7. [DOI] [PubMed] [Google Scholar]
- Wu Z. A., Murphy C., Callan H. G., Gall J. G. Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: loops, spheres, and snurposomes. J Cell Biol. 1991 May;113(3):465–483. doi: 10.1083/jcb.113.3.465. [DOI] [PMC free article] [PubMed] [Google Scholar]