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

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 Lett

journal_title

FEBS letters

authors

Kim TH,Hwang SB,Jeong PY,Lee J,Cho JW

doi

10.1016/j.febslet.2004.11.044

keywords:

subject

Has Abstract

pub_date

2005-01-03 00:00:00

pages

53-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(04)01423-1

journal_volume

579

pub_type

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