TY - JOUR
T1 - Identification and visualization of the sexual agglutinin from the mating-type plus flagellar membrane of Chlamydomonas
AU - Adair, W. Steven
AU - Hwang, Carol
AU - Goodenough, Ursula W.
N1 - Funding Information:
Preliminary experiments on agglutinin identificatron that inspired thus work were performed in thus laboratory by Dr Brian C. Monk. This research was supported by Grants GM-26117 and GM-26150 to U. W. G. from the National Institutes of Health. The electron microscopy was supported by Grant GM-29647 to Dr. John E. Heuser. We thank Dr. Heuser and Fiobyn Carmody for their excellent technical assistance.
PY - 1983/5
Y1 - 1983/5
N2 - Sexual agglutinins located on the flagellar membranes of Chlamydomonas gametes mediate a mating-type-specific adhesion reaction that brings complementary gametes together for zygotic cell fusion. We identify the mating-type plus agglutinin, using a combination of biochemical and genetic analysis, as a glycopolypeptide with an apparent molecular weight of >106 by SDS-polyacylamide gel electrophoresis. Its core polypeptide migrates as a ∼480-kd species, and it is estimated to be present in ∼30 copies per gametic flagellum. The agglutinin is present in the wild type, in a mutant that agglutinates but cannot fuse, and in a complementing diploid, whereas it is absent from four nonagglutinating mutants and from a noncomplementing diploid. Electron microscopy shows the purified agglutinin to be a highly asymmetric molecule, 220 × 4 nm. To our knowledge, this is the first reported purification and visualization of a membrane-associated cell-cell recognition protein.
AB - Sexual agglutinins located on the flagellar membranes of Chlamydomonas gametes mediate a mating-type-specific adhesion reaction that brings complementary gametes together for zygotic cell fusion. We identify the mating-type plus agglutinin, using a combination of biochemical and genetic analysis, as a glycopolypeptide with an apparent molecular weight of >106 by SDS-polyacylamide gel electrophoresis. Its core polypeptide migrates as a ∼480-kd species, and it is estimated to be present in ∼30 copies per gametic flagellum. The agglutinin is present in the wild type, in a mutant that agglutinates but cannot fuse, and in a complementing diploid, whereas it is absent from four nonagglutinating mutants and from a noncomplementing diploid. Electron microscopy shows the purified agglutinin to be a highly asymmetric molecule, 220 × 4 nm. To our knowledge, this is the first reported purification and visualization of a membrane-associated cell-cell recognition protein.
UR - http://www.scopus.com/inward/record.url?scp=0020538471&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(83)90347-1
DO - 10.1016/0092-8674(83)90347-1
M3 - Article
C2 - 6678609
AN - SCOPUS:0020538471
SN - 0092-8674
VL - 33
SP - 183
EP - 193
JO - Cell
JF - Cell
IS - 1
ER -