| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 19, 15768-15775, May 11, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the a-Agglutinin from Saccharomyces
cerevisiae is a cell adhesion glycoprotein expressed on the
surface of cells of a mating type and consists of an anchorage subunit
Aga1p and a receptor binding subunit Aga2p. Cell wall attachment of
Aga2p is mediated through two disulfide bonds to Aga1p (Cappellaro, C.,
Baldermann, C., Rachel, R., and Tanner, W. (1994) EMBO J. 13, 4737-4744). We report here that purified Aga2p was unstable and
had low molar specific activity relative to its receptor
Delineation of Functional Regions within the Subunits of the
Saccharomyces cerevisiae Cell Adhesion Molecule
a-Agglutinin*
§,§,,
,
Department of Biological Sciences and the
Institute for Biomolecular Structure and Function, Hunter College of
the City University of New York, New York 10021 and the
¶ Department of Microbiology and Molecular Genetics, University of
Vermont, Burlington, Vermont 05405
-agglutinin. Aga2p co-expressed with a 149-residue fragment of Aga1p
formed a disulfide-linked complex with specific activity 43-fold higher
than Aga2p expressed alone. Circular dichroism of the complex revealed
a mixed /
structure, whereas Aga2p alone had no periodic
secondary structure. A 30-residue Cys-rich Aga1p fragment was partially
active in stabilization of Aga2p activity. Mutation of either or both
Aga2p cysteine residues eliminated stabilization of Aga2p. Thus the
roles of Aga1p include both cell wall anchorage and
cysteine-dependent conformational restriction of the
binding subunit Aga2p. Mutagenesis of AGA2 identified only
C-terminal residues of Aga2p as being essential for binding activity.
Aga2p residues 45-72 are similar to sequences in soybean
Nod genes, and include residues implicated in
interactions with both Aga1p (including Cys68) and
-agglutinin.
*
Supported by the Grants 1R01-GM47176 and 2SO6-GM60654 from
NIGMS, National Institute of Health (NIH) and by Grant RR-03037 from
the Research Centers in Minority Institutions Program of NIH.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Anesthesia Research Laboratories, Brigham and
Women's Hospital, Harvard Medical School, Boston, MA 02115.
**
Prestent address: Genencor International, P. O. Box 218, 2300 AE,
Leiden, Netherlands.
To whom correspondence should be addressed: Dept. of
Biological Sciences, Hunter College, 695 Park Ave., New York, NY 10021. Tel.: 212-772-5235; Fax: 212-772-5227; E-mail:
lipke@genectr.hunter.cuny.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  A. M. Dranginis, J. M. Rauceo, J. E. Coronado, and P. N. Lipke A Biochemical Guide to Yeast Adhesins: Glycoproteins for Social and Antisocial Occasions Microbiol. Mol. Biol. Rev., June 1, 2007; 71(2): 282 - 294. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. J. Ferris, S. Waffenschmidt, J. G. Umen, H. Lin, J.-H. Lee, K. Ishida, T. Kubo, J. Lau, and U. W. Goodenough Plus and Minus Sexual Agglutinins from Chlamydomonas reinhardtii PLANT CELL, February 1, 2005; 17(2): 597 - 615. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. Huang, M. Zhang, and S. E. Erdman Posttranslational Modifications Required for Cell Surface Localization and Function of the Fungal Adhesin Aga1p Eukaryot. Cell, October 1, 2003; 2(5): 1099 - 1114. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
