The Chlamydomonas cell wall degrading enzyme, lysin, acts on two substrates within the framework of the wall

The Chlamydomonas cell wall is a multilayered, extracellular matrix containing 20-25 proteins and glycoproteins, many of which are highly enriched in hydroxyproline. 80-90% of the wall protein is located in a crystalline portion of the wall that is soluble in sarkosyl-urea solutions as well as in ch...

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Bibliographic Details
Published in:The Journal of cell biology 1988-06, Vol.106 (6), p.2211-2221
Main Authors: Imam, S.H, Snell, W.J
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ALGAE
ALGUE
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Cell biology
Cell Wall - metabolism
CELL WALLS
Cells
Centrifugation
Chlamydomonas
Chlamydomonas - enzymology
Chlamydomonas - ultrastructure
CHLAMYDOMONAS REINHARDTII
CULTURE MEDIA
Detergents
Electron microscopy
ENZIMAS
ENZYME
ENZYMES
Enzymes and enzyme inhibitors
ENZYMIC ACTIVITY
Fundamental and applied biological sciences. Psychology
Gametes
Gels
Hydrolases
Imams
MEDIO DE CULTIVO
MILIEU DE CULTURE
Molecular Weight
Molecules
Mucoproteins - metabolism
PARED CELULAR
PAROI CELLULAIRE
Plant Proteins - metabolism
Solubility
Urea
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Summary:The Chlamydomonas cell wall is a multilayered, extracellular matrix containing 20-25 proteins and glycoproteins, many of which are highly enriched in hydroxyproline. 80-90% of the wall protein is located in a crystalline portion of the wall that is soluble in sarkosyl-urea solutions as well as in chaotropic salts. Although the wall has no cellulose it contains a noncrystalline, highly insoluble framework portion that is responsible for the integrity and overall shape of the wall. In the present report we show that the framework of the wall is composed of two components that are acted upon by lysin, a wall degrading enzyme released by mating gametes. One, which makes up the major portion of the framework, is insoluble upon boiling in SDS-PAGE sample buffer. Lysin treatment of this portion leads to its physical degradation and the concomitant appearance of several SDS-dithiothreitol-soluble polypeptides ranging in relative molecular mass from >400,000 to
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.106.6.2211