ZFIN ID: ZDB-PUB-080306-7
Nuclear localization, DNA binding and restricted expression in neural and germ cells of zebrafish Dmrt3
Li, Q., Zhou, X., Guo, Y., Shang, X., Chen, H., Lu, H., Cheng, H., and Zhou, R.
Date: 2008
Source: Biology of the cell   100(8): 453-463 (Journal)
Registered Authors: Chen, Hao, Li, Qin
Keywords: none
MeSH Terms:
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Nucleus/metabolism*
  • DNA Primers/chemistry
  • DNA-Binding Proteins/metabolism
  • Embryo, Nonmammalian
  • Female
  • In Situ Hybridization
  • Male
  • Molecular Sequence Data
  • Neurons/metabolism
  • Nuclear Localization Signals
  • Ovary/metabolism
  • Phylogeny
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Testis/metabolism
  • Transcription Factors/chemistry
  • Transcription Factors/genetics*
  • Transcription Factors/metabolism*
  • Zebrafish/embryology
  • Zebrafish Proteins/chemistry
  • Zebrafish Proteins/genetics*
  • Zebrafish Proteins/metabolism*
PubMed: 18282142 Full text @ Biol. Cell
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ABSTRACT
Background information. The DM (Doublesex and Male aberrant-3) genes implicated in sexual development in diverse metazoan organisms have been proved to be involved in development of non-gonadal tissues. The aim of the present study was to identify and characterize Dmrt3 of zebrafish. Results. Zebrafish Dmrt3 has a conserved DMA domain, besides a common DM domain, which clustered it into the DMRTA subfamily. During embryogenesis, Dmrt3 expression increases gradually to a high level at pharyngula stage, which is restricted in the olfactory placode and the neural tube. In the juvenile zebrafish, the gene expression is first detected in undifferentiated gonad at 17-day post fertilization. In adult, Dmrt3 expresses only in the developing germ cells of both gonads, mainly in spermatogonia, spermatocytes and developing oocytes. The Dmrt3 has a functional nuclear localization signal (NLS) 41KGHKR45 within the DM domain, which ensures to exert its role in the nucleus. Moreover, electrophoretic mobility shift assay (EMSA) indicates that the Dmrt3-derived DM polypeptide binds to similar sites of both targets of DSX (Doublesex) and MAB-3 (Male aberrant-3). Conclusion. These results suggest that as a DNA binding protein, zebrafish Dmrt3 may function in the nucleus as a potential transcription factor to exert potential roles in the development of the olfactory placode, the neural tube and germ cells.
ADDITIONAL INFORMATION