Skip to main content
Genetics logoLink to Genetics
. 2000 Feb;154(2):713–724. doi: 10.1093/genetics/154.2.713

Functional domains of the Drosophila bicaudal-D protein.

J Oh 1, K Baksa 1, R Steward 1
PMCID: PMC1460953  PMID: 10655224

Abstract

The localization of oocyte-specific determinants in the form of mRNAs to the pro-oocyte is essential for the establishment of oocyte identity. Localization of the Bicaudal-D (Bic-D) protein to the presumptive oocyte is required for the accumulation of Bic-D and other mRNAs to the pro-oocyte. The Bic-D protein contains four well-defined heptad repeat domains characteristic of intermediate filament proteins, and several of the mutations in Bic-D map to these conserved domains. We have undertaken a structure-function analysis of Bic-D by testing the function of mutant Bic-D transgenes (Bic-D(H)) deleted for each of the heptad repeat domains in a Bic-D null background. Our transgenic studies indicate that only the C-terminal heptad repeat deletion results in a protein that has lost zygotic and ovarian functions. The three other deletions result in proteins with full zygotic function, but with affected ovarian function. The functional importance of each domain is well correlated with its conservation in evolution. The analysis of females heterozygous for Bic-D(H) and the existing alleles Bic-D(PA66) or Bic-D(R26) reveals that Bic-D(R26) as well as some of Bic-D(H) transgenes have antimorphic effects. The yeast two-hybrid interaction assay shows that Bic-D forms homodimers. Furthermore, we found that Bic-D exists as a multimeric protein complex consisting of Egl and at least two Bic-D monomers.

Full Text

The Full Text of this article is available as a PDF (359.9 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baens M., Marynen P. A human homologue (BICD1) of the Drosophila bicaudal-D gene. Genomics. 1997 Nov 1;45(3):601–606. doi: 10.1006/geno.1997.4971. [DOI] [PubMed] [Google Scholar]
  2. Brown J. H., Cohen C., Parry D. A. Heptad breaks in alpha-helical coiled coils: stutters and stammers. Proteins. 1996 Oct;26(2):134–145. doi: 10.1002/(SICI)1097-0134(199610)26:2<134::AID-PROT3>3.0.CO;2-G. [DOI] [PubMed] [Google Scholar]
  3. Ephrussi A., Dickinson L. K., Lehmann R. Oskar organizes the germ plasm and directs localization of the posterior determinant nanos. Cell. 1991 Jul 12;66(1):37–50. doi: 10.1016/0092-8674(91)90137-n. [DOI] [PubMed] [Google Scholar]
  4. Gietz D., St Jean A., Woods R. A., Schiestl R. H. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 1992 Mar 25;20(6):1425–1425. doi: 10.1093/nar/20.6.1425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Lantz V., Ambrosio L., Schedl P. The Drosophila orb gene is predicted to encode sex-specific germline RNA-binding proteins and has localized transcripts in ovaries and early embryos. Development. 1992 May;115(1):75–88. doi: 10.1242/dev.115.1.75. [DOI] [PubMed] [Google Scholar]
  6. Mach J. M., Lehmann R. An Egalitarian-BicaudalD complex is essential for oocyte specification and axis determination in Drosophila. Genes Dev. 1997 Feb 15;11(4):423–435. doi: 10.1101/gad.11.4.423. [DOI] [PubMed] [Google Scholar]
  7. McLachlan A. D., Karn J. Periodic features in the amino acid sequence of nematode myosin rod. J Mol Biol. 1983 Mar 15;164(4):605–626. doi: 10.1016/0022-2836(83)90053-0. [DOI] [PubMed] [Google Scholar]
  8. Mohler J., Wieschaus E. F. Dominant maternal-effect mutations of Drosophila melanogaster causing the production of double-abdomen embryos. Genetics. 1986 Apr;112(4):803–822. doi: 10.1093/genetics/112.4.803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ran B., Bopp R., Suter B. Null alleles reveal novel requirements for Bic-D during Drosophila oogenesis and zygotic development. Development. 1994 May;120(5):1233–1242. doi: 10.1242/dev.120.5.1233. [DOI] [PubMed] [Google Scholar]
  10. Ray R. P., Schüpbach T. Intercellular signaling and the polarization of body axes during Drosophila oogenesis. Genes Dev. 1996 Jul 15;10(14):1711–1723. doi: 10.1101/gad.10.14.1711. [DOI] [PubMed] [Google Scholar]
  11. Robertson H. M., Preston C. R., Phillis R. W., Johnson-Schlitz D. M., Benz W. K., Engels W. R. A stable genomic source of P element transposase in Drosophila melanogaster. Genetics. 1988 Mar;118(3):461–470. doi: 10.1093/genetics/118.3.461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schüpbach T., Roth S. Dorsoventral patterning in Drosophila oogenesis. Curr Opin Genet Dev. 1994 Aug;4(4):502–507. doi: 10.1016/0959-437x(94)90064-a. [DOI] [PubMed] [Google Scholar]
  13. Schüpbach T., Wieschaus E. Female sterile mutations on the second chromosome of Drosophila melanogaster. II. Mutations blocking oogenesis or altering egg morphology. Genetics. 1991 Dec;129(4):1119–1136. doi: 10.1093/genetics/129.4.1119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Stuurman N., Häner M., Sasse B., Hübner W., Suter B., Aebi U. Interactions between coiled-coil proteins: Drosophila lamin Dm0 binds to the bicaudal-D protein. Eur J Cell Biol. 1999 Apr;78(4):278–287. doi: 10.1016/s0171-9335(99)80061-2. [DOI] [PubMed] [Google Scholar]
  15. Suter B., Steward R. Requirement for phosphorylation and localization of the Bicaudal-D protein in Drosophila oocyte differentiation. Cell. 1991 Nov 29;67(5):917–926. doi: 10.1016/0092-8674(91)90365-6. [DOI] [PubMed] [Google Scholar]
  16. Sym M., Roeder G. S. Zip1-induced changes in synaptonemal complex structure and polycomplex assembly. J Cell Biol. 1995 Feb;128(4):455–466. doi: 10.1083/jcb.128.4.455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Theurkauf W. E., Alberts B. M., Jan Y. N., Jongens T. A. A central role for microtubules in the differentiation of Drosophila oocytes. Development. 1993 Aug;118(4):1169–1180. doi: 10.1242/dev.118.4.1169. [DOI] [PubMed] [Google Scholar]

Articles from Genetics are provided here courtesy of Oxford University Press

RESOURCES