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(Received for publication, April 4, 1995) From the Expression of polysialic acid (PSA) involves its specific
attachment to the neural cell adhesion molecule (NCAM). Here we
identify the amino acid residues within NCAM that are polysialylated
and structural domains of the NCAM polypeptide that are required for
addition of PSA in cells. Chicken NCAM cDNAs containing amino acid
mutations, domain deletions, and domain substitutions were expressed in
the F11 rat/mouse hybrid cell line, which can produce polysialylated
NCAM. Polysialylation of the chicken NCAM was evaluated by
immunopurification and electrophoresis. Mutation of all three potential N-glycosylation sites within the fifth immunoglobulin domain
(Ig5) abrogated polysialylation. Analysis of paired mutations revealed
that Asn-459 is heavily polysialylated, Asn-430 has a lower level of
substitution, and Asn-404 receives little or no PSA. Analysis of domain
deletions established that the intracellular domain, Ig domains
1-3, and the COOH-terminal fibronectin-type III (FNIII) repeat
are not required for polysialylation, but that deletion of either the
adjacent Ig4 or FNIII-type domain prevented addition of PSA.
Accordingly, a minimal polypeptide for polysialylation was found to
contain Ig domains 4 and 5, the adjacent FNIII repeat, plus a membrane
attachment. These results suggest that although all PSA is located
within Ig5, regions outside Ig5 also play a role in PSA addition to
NCAM. Furthermore, molecular modeling indicates spatial proximity of
Asn-430 and Asn-459 and a tight-locking arrangement between Ig4, Ig5,
and FNIII#1 that would be consistent with their formation of a
spatially discrete enzyme recognition site for polysialylation.
Volume 270,
Number 29,
Issue of July 21, pp. 17171-17179, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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