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Journal of Molecular Evolution

, Volume 66, Issue 1, pp 1–10 | Cite as

The Lengthening of a Giant Protein: When, How, and Why?

  • Olivier Meiniel
  • Robert Meiniel
  • Fabrice Lalloué
  • Robert Didier
  • Marie-Odile Jauberteau
  • Annie Meiniel
  • Daniel Petit
Article

Abstract

Subcommissural organ (SCO)-spondin is a giant glycoprotein of more than 5000 amino acids found in Vertebrata, expressed in the central nervous system and constitutive of Reissner’s fiber. For the first time, in situ hybridization performed on zebrafish (Danio rerio) embryos shows that the gene encoding this protein is expressed transitionally in the floor plate, the ventral midline of the neural tube, and later in the diencephalic third ventricle roof, the SCO. The modular organization of the protein in Echinodermata (Strongylocentrotus purpuratus), Urochordata (Ciona savignyi and C. intestinalis), and Vertebrata (Teleostei, Amphibia, Aves and Mammalia) is also described. As the thrombospondin type 1 repeat motifs represent an increasingly large part of the protein during Deuterostomia evolution, the duplication mechanisms leading to this complex organization are examined. The functional significance of the particularly well-preserved arrangement of the series of SCO-spondin repeat motifs and thombospondin type 1 repeats is discussed.

Keywords

SCO-spondin Central nervous system Thrombospondin type 1 repeat SCO-spondin repeat Deuterostomia 

Notes

Acknowledgments

We thank Sridhar Ramachandran of the ZFIN for editing the scospondin gene. We acknowledge the contributions of genome sequencing projects that have generated some sequences useful for our analyses. Special thanks go to Olivier Jaillon at the Genoscope for providing T. nigroviridis sequencing accession numbers and to Kerstin Howe and Mario Caccamo at Sanger for helping with D. rerio genomic data. We are grateful to Bernard and Christine Thisse for their generous collaboration in establishing zebrafish expression patterns. We thank Richard Ryan for proofreading. Work at the UMR 384 is supported by INSERM. O. Meiniel is supported by a DRRT postdoctoral fellowship (FNADT, Région Auvergne-Limousin).

Supplementary material

239_2007_9055_MOESM1_ESM.doc (66 kb)
(DOC 66 kb)

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Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  • Olivier Meiniel
    • 1
  • Robert Meiniel
    • 1
  • Fabrice Lalloué
    • 2
  • Robert Didier
    • 1
  • Marie-Odile Jauberteau
    • 2
  • Annie Meiniel
    • 1
  • Daniel Petit
    • 3
  1. 1.Faculté de MédecineINSERM, UMR 384Clermont-Ferrand cedexFrance
  2. 2.Faculty of MedicineEA 3842Limoges cedexFrance
  3. 3.INRA, UMR 1061Université de LimogesLimoges cedexFrance

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