Gene Networks Database
Hemicentrotus pulcherrimus Genes in Development: Arylsulfatase
In sea urchin embryos arylsulfatase makes up as much as 0.5% of the total protein of the pluteus larva.
Arylsulfatase may be a structural component
of the extracellular matrices involved in cell movement during morphogenesis (Rapraeger et al., 1981).
A sequence of 551 amino acids was deduced from the arylsulfatase
nucleotide sequence. The amino terminal region is rich in hydrophobic
amino acids which is characteristic of a signal peptide.
It was estimated that the 21th is the amino terminal of sea urchin arylsulfatase. The molecular mass of the arylsulfatase starting from the
21th glutamine was calculated to be 58827 Da, which is about 4 kDa
smaller than that of the subunit (63 kDa) estimated by SDS/polyacrylamide gel electrophoresis (the difference in molecular mass may be due to the glucosylation of the polypeptide).
No protein sequences similar to the deduced arylsulfatase sequence
were found (Sasaki et al., 1988).
In sea urchin embryos arylsulfatase is localized in both the cytoplasm
and extracellular matrices (Rapraeger et al., 1981).
Nothern blot analysis showed that there are two mRNAs for arylsulfatase,
2.9-kb RNA (major) and a 1.7-kb RNA (minor). The 2.9-kb RNA seems to be
a true mRNA for arylsulfatase; the 1.7-kb RNA is probably a specific degradation product of the large mRNA, or it contains a region of close
homology to part of the 3` end of the gene.
The unfertilized egg contains a small amount of 2.9-kb mRNA.
This amount gradually decreases until the unhatched blastula stage.
After hatching, the 2.9-kb mRNA starts to increase drastically.
The concentration of arylsulfatase mRNA increases about 2000-fold
during development between the 32-cell stage and the prism stage (Sasaki et al., 1988).
Method: Nothern blot analysis
Reference: Sasaki et al., 1988
Comments are welcome to Sveta Surkova
Copyright © 1997 GeNet Team