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. 1989 Jun;9(6):2756–2760. doi: 10.1128/mcb.9.6.2756

Expression of the poly(A)-binding protein during development of Xenopus laevis.

B D Zelus 1, D H Giebelhaus 1, D W Eib 1, K A Kenner 1, R T Moon 1
PMCID: PMC362352  PMID: 2761544

Abstract

We have isolated and sequenced cDNA clones encoding the poly(A)-binding protein of Xenopus laevis oocytes. Polyclonal antiserum was raised against a fusion protein encoding 185 amino acids of the Xenopus poly(A)-binding protein. This antiserum localizes the poly(A)-binding protein to subcellular sites associated with protein synthesis; in the retina, immunoreactive protein is detected in the synthetically active inner segment of the photoreceptor but not in the transductive outer segment. Transcripts encoding the poly(A)-binding protein are present in oocytes, although no protein is detected on protein blots. In contrast, the levels of both transcripts and protein increase in development, which correlates with the observed increase in total poly(A) during Xenopus embryogenesis (N. Sagata, K. Shiokawa, and K. Yamana, Dev. Biol. 77:431-448, 1980).

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Selected References

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  1. Adam S. A., Nakagawa T., Swanson M. S., Woodruff T. K., Dreyfuss G. mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Mol Cell Biol. 1986 Aug;6(8):2932–2943. doi: 10.1128/mcb.6.8.2932. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baer B. W., Kornberg R. D. The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein. J Cell Biol. 1983 Mar;96(3):717–721. doi: 10.1083/jcb.96.3.717. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blobel G. A protein of molecular weight 78,000 bound to the polyadenylate region of eukaryotic messenger RNAs. Proc Natl Acad Sci U S A. 1973 Mar;70(3):924–928. doi: 10.1073/pnas.70.3.924. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Doel M. T., Carey N. H. The translational capacity of deadenylated ovalbumin messenger RNA. Cell. 1976 May;8(1):51–58. doi: 10.1016/0092-8674(76)90184-7. [DOI] [PubMed] [Google Scholar]
  5. Drummond D. R., Armstrong J., Colman A. The effect of capping and polyadenylation on the stability, movement and translation of synthetic messenger RNAs in Xenopus oocytes. Nucleic Acids Res. 1985 Oct 25;13(20):7375–7394. doi: 10.1093/nar/13.20.7375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  7. Galili G., Kawata E. E., Smith L. D., Larkins B. A. Role of the 3'-poly(A) sequence in translational regulation of mRNAs in Xenopus laevis oocytes. J Biol Chem. 1988 Apr 25;263(12):5764–5770. [PubMed] [Google Scholar]
  8. Giebelhaus D. H., Eib D. W., Moon R. T. Antisense RNA inhibits expression of membrane skeleton protein 4.1 during embryonic development of Xenopus. Cell. 1988 May 20;53(4):601–615. doi: 10.1016/0092-8674(88)90576-4. [DOI] [PubMed] [Google Scholar]
  9. Giebelhaus D. H., Zelus B. D., Henchman S. K., Moon R. T. Changes in the expression of alpha-fodrin during embryonic development of Xenopus laevis. J Cell Biol. 1987 Aug;105(2):843–853. doi: 10.1083/jcb.105.2.843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Grange T., de Sa C. M., Oddos J., Pictet R. Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif. Nucleic Acids Res. 1987 Jun 25;15(12):4771–4787. doi: 10.1093/nar/15.12.4771. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Grossi de Sa M. F., Standart N., Martins de Sa C., Akhayat O., Huesca M., Scherrer K. The poly(A)-binding protein facilitates in vitro translation of poly(A)-rich mRNA. Eur J Biochem. 1988 Oct 1;176(3):521–526. doi: 10.1111/j.1432-1033.1988.tb14309.x. [DOI] [PubMed] [Google Scholar]
  12. Gurdon J. B., Wickens M. P. The use of Xenopus oocytes for the expression of cloned genes. Methods Enzymol. 1983;101:370–386. doi: 10.1016/0076-6879(83)01028-9. [DOI] [PubMed] [Google Scholar]
  13. HANNA C. CHANGES IN DNA, RNA, AND PROTEIN SYNTHESIS IN THE DEVELOPING LENS. Invest Ophthalmol. 1965 Aug;4:480–495. [PubMed] [Google Scholar]
  14. Harvey R. P., Melton D. A. Microinjection of synthetic Xhox-1A homeobox mRNA disrupts somite formation in developing Xenopus embryos. Cell. 1988 Jun 3;53(5):687–697. doi: 10.1016/0092-8674(88)90087-6. [DOI] [PubMed] [Google Scholar]
  15. Huez G., Bruck C., Cleuter Y. Translational stability of native and deadenylylated rabbit globin mRNA injected into HeLa cells. Proc Natl Acad Sci U S A. 1981 Feb;78(2):908–911. doi: 10.1073/pnas.78.2.908. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Jacobson A., Favreau M. Possible involvement of poly(A) in protein synthesis. Nucleic Acids Res. 1983 Sep 24;11(18):6353–6368. doi: 10.1093/nar/11.18.6353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Larson D. E., Sells B. H. The function of proteins that interact with mRNA. Mol Cell Biochem. 1987 Mar;74(1):5–15. doi: 10.1007/BF00221907. [DOI] [PubMed] [Google Scholar]
  18. Melton D. A., Krieg P. A., Rebagliati M. R., Maniatis T., Zinn K., Green M. R. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 1984 Sep 25;12(18):7035–7056. doi: 10.1093/nar/12.18.7035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Moon R. T., Ngai J., Wold B. J., Lazarides E. Tissue-specific expression of distinct spectrin and ankyrin transcripts in erythroid and nonerythroid cells. J Cell Biol. 1985 Jan;100(1):152–160. doi: 10.1083/jcb.100.1.152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
  21. Rebagliati M. R., Weeks D. L., Harvey R. P., Melton D. A. Identification and cloning of localized maternal RNAs from Xenopus eggs. Cell. 1985 Oct;42(3):769–777. doi: 10.1016/0092-8674(85)90273-9. [DOI] [PubMed] [Google Scholar]
  22. Sachs A. B., Bond M. W., Kornberg R. D. A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Cell. 1986 Jun 20;45(6):827–835. doi: 10.1016/0092-8674(86)90557-x. [DOI] [PubMed] [Google Scholar]
  23. Sagata N., Shiokawa K., Yamana K. A study on the steady-state population of poly(A)+RNA during early development of Xenopus laevis. Dev Biol. 1980 Jun 15;77(2):431–448. doi: 10.1016/0012-1606(80)90486-8. [DOI] [PubMed] [Google Scholar]
  24. Sanger F. Determination of nucleotide sequences in DNA. Science. 1981 Dec 11;214(4526):1205–1210. doi: 10.1126/science.7302589. [DOI] [PubMed] [Google Scholar]
  25. Setyono B., Greenberg J. R. Proteins associated with poly(A) and other regions of mRNA and hnRNA molecules as investigated by crosslinking. Cell. 1981 Jun;24(3):775–783. doi: 10.1016/0092-8674(81)90103-3. [DOI] [PubMed] [Google Scholar]
  26. Shapiro R. A., Herrick D., Manrow R. E., Blinder D., Jacobson A. Determinants of mRNA stability in Dictyostelium discoideum amoebae: differences in poly(A) tail length, ribosome loading, and mRNA size cannot account for the heterogeneity of mRNA decay rates. Mol Cell Biol. 1988 May;8(5):1957–1969. doi: 10.1128/mcb.8.5.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Swanson M. S., Nakagawa T. Y., LeVan K., Dreyfuss G. Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins. Mol Cell Biol. 1987 May;7(5):1731–1739. doi: 10.1128/mcb.7.5.1731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Swiderski R. E., Richter J. D. Photocrosslinking of proteins to maternal mRNA in Xenopus oocytes. Dev Biol. 1988 Aug;128(2):349–358. doi: 10.1016/0012-1606(88)90297-7. [DOI] [PubMed] [Google Scholar]
  29. Zeevi M., Nevins J. R., Darnell J. E., Jr Newly formed mRNA lacking polyadenylic acid enters the cytoplasm and the polyribosomes but has a shorter half-life in the absence of polyadenylic acid. Mol Cell Biol. 1982 May;2(5):517–525. doi: 10.1128/mcb.2.5.517. [DOI] [PMC free article] [PubMed] [Google Scholar]

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