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Volume 270,
Number 44,
Issue of November 3, 1995 pp. 26168-26177
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Structure of Saccharomyces cerevisiae -Agglutinin
EVIDENCE FOR A YEAST CELL WALL PROTEIN WITH MULTIPLE
IMMUNOGLOBULIN-LIKE DOMAINS WITH ATYPICAL DISULFIDES
(Received for publication, June
1, 1995; and in revised form, August 8, 1995)
Min-Hao
Chen
,
Zheng-Ming
Shen
,
Stephen
Bobin
,
Peter C.
Kahn
,
Peter
N.
Lipke
-Agglutinin of Saccharomyces cerevisiae is a cell
wall-associated protein that mediates cell interaction in mating.
Although the mature protein includes about 610 residues, the
NH -terminal half of the protein is sufficient for binding
to its ligand a-agglutinin. -Agglutinin , a
fully active fragment of the protein, has been purified and analyzed.
Circular dichroism spectroscopy, together with sequence alignments,
suggest that -agglutinin consists of three
immunoglobulin variable-like domains: domain I, residues 20-104;
domain II, residues 105-199; and domain III, residues
200-326. Peptide sequencing data established the arrangement of
the disulfide bonds in -agglutinin .
Cys is disulfide-bonded to Cys , forming an
interdomain bond between domains I and II. Cys is bonded
to Cys , in an atypical intradomain disulfide bond between
the A and F strands of domain III. Cys and Cys have free sulfhydryls. Sequencing also showed that at least two
of three potential N-glycosylation sites with sequence
Asn-Xaa-Thr are glycosylated. At least one of three Asn-Xaa-Ser
sequences is not glycosylated. No residues NH -terminal to
Ser were O-glycosylated, whereas
Ser , and all hydroxy amino acid residues COOH-terminal to
this position were modified. Therefore O-glycosylated Ser and
Thr residues cluster in the COOH-terminal region of domain III, and the O-glycosylation continues into a Ser/Thr-rich sequence that
extends from domain III to the COOH-terminal of the full-length
protein.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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