Requirement of tyrosylprotein sulfotransferase-A for proper cuticle formation in the nematode C. elegans

FEBS Lett. 2005 Jan 3;579(1):53-8. doi: 10.1016/j.febslet.2004.11.044.

Abstract

Tyrosine O-sulfation is one of the post-translational modification processes that occur to membrane proteins and secreted proteins in eukaryotes. Tyrosylprotein sulfotransferase (TPST) is responsible for this modification, and in this report, we describe the expression pattern and the biological role of TPST-A in the nematode Caenorhabditis elegans. We found that TPST-A was mainly expressed in the hypodermis, especially in the seam cells. Reduction of TPST-A activity by RNAi caused severe defects in cuticle formation, indicating that TPST-A is involved in the cuticle formation in the nematode. We found that RNAi of TPST-A suppressed the roller phenotype caused by mutations in the rol-6 collagen gene, suggesting that sulfation of collagen proteins may be important for proper organization of the extracellular cuticle matrix. The TPST-A RNAi significantly decreased the dityrosine level in the worms, raising the possibility that the sulfation process may be a pre-requisite for the collagen tyrosine cross-linking.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caenorhabditis elegans / embryology
  • Caenorhabditis elegans / enzymology*
  • Caenorhabditis elegans / growth & development
  • Caenorhabditis elegans Proteins / analysis
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Caenorhabditis elegans Proteins / physiology*
  • Collagen / genetics
  • Collagen / metabolism
  • Gene Expression / drug effects
  • Gene Expression / genetics
  • Green Fluorescent Proteins / analysis
  • Green Fluorescent Proteins / genetics
  • Mutation / genetics
  • Protein Processing, Post-Translational*
  • RNA, Small Interfering / genetics
  • RNA, Small Interfering / pharmacology
  • Subcutaneous Tissue / chemistry
  • Subcutaneous Tissue / metabolism
  • Sulfotransferases / genetics
  • Sulfotransferases / metabolism
  • Sulfotransferases / physiology*
  • Tyrosine / analogs & derivatives*
  • Tyrosine / analysis
  • Tyrosine / metabolism

Substances

  • Caenorhabditis elegans Proteins
  • RNA, Small Interfering
  • enhanced green fluorescent protein
  • rol-6 protein, C elegans
  • Green Fluorescent Proteins
  • Tyrosine
  • Collagen
  • dityrosine
  • Sulfotransferases
  • tpst-1 protein, C elegans