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Requirement of tyrosylprotein sulfotransferase‐A for proper cuticle formation in the nematode C. elegans
Author(s) -
Kim Tai Hoon,
Hwang Soon Baek,
Jeong Pan-Young,
Lee Junho,
Cho Jin Won
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.044
Subject(s) - sulfation , cuticle (hair) , caenorhabditis elegans , rna interference , microbiology and biotechnology , extracellular matrix , phenotype , nematode , tyrosine , biology , chemistry , biochemistry , gene , genetics , rna , ecology
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.