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Vol. 9, Issue 2, 291-300, February 1998
and
*Friedrich Miescher-Institut, CH-4002 Basel, Switzerland;
C-mannosylation of Trp-7 in human ribonuclease 2 (RNase 2) is a novel kind of protein glycosylation that differs
fundamentally from N- and O-glycosylation
in the protein-sugar linkage. Previously, we established that the
specificity determinant of the acceptor substrate (RNase 2) consists of
the sequence W-x-x-W, where the first Trp becomes
C-mannosylated. Here we investigated the reaction with
respect to the mannosyl donor and the involvement of a
glycosyltransferase. C-mannosylation of Trp-7 was reduced 10-fold in CHO (Chinese hamster ovary) Lec15 cells, which are deficient
in dolichyl-phosphate-mannose (Dol-P-Man) synthase activity, compared
with wild-type cells. This was not a result of a decrease in
C-mannosyltransferase activity. Rat liver microsomes were
used to C-mannosylate the N-terminal
dodecapeptide from RNase 2 in vitro, with Dol-P-Man as the donor. This
microsomal transferase activity was destroyed by heat and protease
treatment, and displayed the same acceptor substrate specificity as the
in vivo reaction studied previously. The C-C linkage between the indole
and the mannosyl moiety was demonstrated by tandem electrospray mass
spectrometry analysis of the product. GDP-Man, in the presence of
Dol-P, functioned as a precursor in vitro with membranes from wild-type
but not CHO Lec15 cells. In contrast, with Dol-P-Man both membrane
preparations were equally active. It is concluded that a microsomal
transferase catalyses C-mannosylation of Trp-7, and that the
minimal biosynthetic pathway can be defined as: Man -> -> GDP-Man
-> Dol-P-Man -> (C2-Man-)Trp.
UNMR 111 du CNRS, Laboratoire de Chimie Biologique,
Université des Sciences et Technologies de Lille, France
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