beta-Glucan synthesis in the cotton fiber. III. Identification of UDP-glucose-binding subunits of beta-glucan synthases by photoaffinity labeling with [beta-32P]5'-N3-UDP-glucose

Using differential product entrapment and photolabeling under specifying conditions, we identified a 37-kD polypeptide as the best candidate among the UDP-glucose-binding polypeptides for the catalytic subunit of cotton (Gossypium hirsutum) cellulose synthase. This polypeptide is enriched by entrapm...

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Published inPlant physiology (Bethesda) Vol. 101; no. 4; pp. 1149 - 1156
Main Authors Li, L, Drake, R.R. Jr, Clement, S, Brown, R.M. Jr
Format Journal Article
LanguageEnglish
Published Rockville, MD American Society of Plant Physiologists 01.04.1993
Subjects
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Agronomy. Soil science and plant productions
Beets
Biological and medical sciences
Biosynthesis
Calcium
CELLULOSE
CELULOSA
Cotton fibers
Enzymes
Fundamental and applied biological sciences. Psychology
GLICOSILTRANSFERASAS
GLUCANE
GLUCANO
Glucans
GLUCOSA
GLUCOSE
GLYCOSYLTRANSFERASE
GOSSYPIUM HIRSUTUM
Immunology
Magnesium
Metabolism
Metabolism and Enzymology
METABOLISME DES GLUCIDES
METABOLISMO DE CARBOHIDRATOS
NUCLEOTIDE
NUCLEOTIDOS
PELOS VEGETALES
Photosynthesis, respiration. Anabolism, catabolism
Plant physiology and development
Plants
POIL VEGETAL
Product labeling
Malvaceae
Cellulose
Plant fiber
Biosynthesis
Glucose
Photoaffinity labelling
Fiber crop
Effector
Characterization
Glucan
Binding protein
Enzymatic activity
Dicotyledones
Angiospermae
pH
Spermatophyta
Gossypium hirsutum
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Summary:Using differential product entrapment and photolabeling under specifying conditions, we identified a 37-kD polypeptide as the best candidate among the UDP-glucose-binding polypeptides for the catalytic subunit of cotton (Gossypium hirsutum) cellulose synthase. This polypeptide is enriched by entrapment under conditions favoring beta-1,4-glucan synthesis, and it is magnesium dependent and sensitive to unlabeled UDP-glucose. A 52-kD polypeptide was identified as the most likely candidate for the catalytic subunit of beta-1,3-glucan synthase because this polypeptide is the most abundant protein in the entrapment fraction obtained under conditions favoring beta-1,3-glucan synthesis, is coincident with beta-1,3-glucan synthase activity, and is calcium dependent. The possible involvement of other polypeptides in the synthesis of beta-1,3-glucan is discussed
Bibliography:F60
9428770
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.101.4.1149