CC-2691 L-23 (pf18 derivative)
$30.00
From Robert Bloodgood, University of Virginia, April 1992
Phenotype: impaired motility
L-23 is a Chlamydomonas mutant obtained by MNNG mutagenesis of pf-18 followed by cell sorting. It has totally lost binding of a monoclonal antibody to an N-linked carbohydrate epitope on FMG-1B, exhibits normal binding of a monoclonal antibody to a protein epitope on FMG-1B and exhibits greatly increased binding of concanavalin A. This suggests a glycosylation mutant that results in a high mannose form (instead of the normal complex carbohydrate form) at the many glycosylation sites on FMG-1B (the major flagellar membrane glycoprotein) as well on other glycoproteins. Unpublished preliminary data from a Spanish carbohydrate lab suggest that this strain has a mutation in a mannosidase enzyme.
Bloodgood RA, Salomonsky NL, Reinhart FD (1987) Use of carbohydrate probes in conjunction with fluorescence-activated cell sorting to select mutant cell lines of Chlamydomonas with defects in cell surface glycoproteins. Exp Cell Res 173:572-585
Bloodgood RA, Salomonsky NL (1989) Use of a novel Chlamydomonas mutant to demonstrate that flagellar glycoprotein movements are necessary for the expression of gliding motility. Cell Motil Cytoskeleton 13:1-8