PUBLICATION

Identification and Characterization of Evolutionarily Conserved Pufferfish, Zebrafish, and Frog Orthologs of GASZ

Authors
Yan, W., Ma, L., Zilinski, C.A., and Matzuk, M.M.
ID
ZDB-PUB-040216-14
Date
2004
Source
Biology of reproduction   70(6): 1619-1625 (Journal)
Registered Authors
Keywords
germ cells, meiosis, haploid, spermatogenesis
MeSH Terms
  • Adaptor Proteins, Signal Transducing/chemistry
  • Adaptor Proteins, Signal Transducing/genetics*
  • Amino Acid Sequence
  • Animals
  • Ankyrin Repeat
  • Base Sequence
  • DNA, Complementary/genetics
  • Evolution, Molecular
  • Female
  • Gene Expression
  • Leucine Zippers/genetics
  • Male
  • Molecular Sequence Data
  • Oogenesis/genetics
  • Ovary/metabolism
  • RNA, Messenger/genetics
  • RNA, Messenger/metabolism
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Species Specificity
  • Spermatogenesis/genetics
  • Takifugu/genetics*
  • Testis/metabolism
  • Xenopus Proteins/genetics
  • Xenopus laevis/genetics*
  • Zebrafish/genetics*
  • Zebrafish Proteins/genetics
PubMed
14766731 Full text @ Biol. Reprod.
Abstract
We previously identified Gasz (a germ cell-specific gene encoding a protein containing four ankyrin repeats, a sterile-alpha motif, and a basic leucine zipper) in six mammalian species. Here, we report GASZ orthologs in pufferfish (Fugu rubripes), zebrafish (Danio verio), and frog (Xenopus laevis). Sequences of the three Gasz cDNAs were determined by database mining and 5'- and 3'-RACE followed by sequencing. The three orthologous vertebrate genes encode proteins structurally similar to mammalian GASZ, and contain the characteristic four ankyrin repeats (ANKs) and sterile-alpha motif (SAM). Their ANK and SAM domains share 55%-74% and 38%-55% amino acid identity with those in human GASZ, respectively. Similar to human and mouse Gasz genes, pufferfish Gasz is composed of 13 exons, spanning approximately 12 kb, and flanked by Cftr at its 5'-end and Wnt2 at its 3'-end. Northern and Western blot analyses detect frog Gasz only in testis and ovary. In situ hybridization and immunohistochemical analyses show that frog Gasz mRNA and protein expression is confined to pachytene spermatocytes in the testis and to oocytes in the ovary. In frog oocytes, GASZ protein appears to localize to a cytoplasmic structure resembling the Balbiani body, a postulated mRNA transport organizer in the cytoplasm. The high evolutionary conservation and germ-cell specificity suggest that GASZ plays an essential role in gametogenesis. The data presented here are important for future studies of the physiological roles of GASZ using fish and amphibians as animal models.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping