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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kim TH,Hwang SB,Jeong PY,Lee J,Cho JWdoi
10.1016/j.febslet.2004.11.044keywords:
subject
Has Abstractpub_date
2005-01-03 00:00:00pages
53-8issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(04)01423-1journal_volume
579pub_type
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