Plant polypeptides reversibly glycosylated by UDP-glucose. Possible components of golgi β-glucan synthase in pea cells
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Plant polypeptides reversibly glycosylated by UDP-glucose. Possible components of golgi β-glucan synthase in pea cells. / Dhugga, K. S.; Ulvskov, P.; Gallagher, S. R.; Ray, P. M.
I: Journal of Biological Chemistry, Bind 266, Nr. 32, 1991, s. 21977-21984.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Plant polypeptides reversibly glycosylated by UDP-glucose. Possible components of golgi β-glucan synthase in pea cells
AU - Dhugga, K. S.
AU - Ulvskov, P.
AU - Gallagher, S. R.
AU - Ray, P. M.
PY - 1991
Y1 - 1991
N2 - In pea membranes, UDP[14C]Glc glycosylates a ~40-kDa polypeptide doublet. This label rapidly disappears if excess unlabeled UDP-Glc, or UDP, is added, indicating that the glycosylation is reversible, and suggesting that the glycosylated polypeptides might be intermediates in a glycosyl transfer reaction. Glycosylation of the doublet requires a divalent cation, the effective ions being the same (except for Zn2+) as those that activate Golgi-localized β-glucan synthase (GS-I) activity. Treatments that inhibit GS-I also inhibit doublet glycosylation. The doublet is associated with Golgi (and to a minor extent with plasma) membranes and occurs also in the soluble fraction. The Golgi-bound doublet may be a component of the GS-I system. Immunological, inactivation, and fractionation evidence indicates that at least one other polypeptide is required in GS-I activity.
AB - In pea membranes, UDP[14C]Glc glycosylates a ~40-kDa polypeptide doublet. This label rapidly disappears if excess unlabeled UDP-Glc, or UDP, is added, indicating that the glycosylation is reversible, and suggesting that the glycosylated polypeptides might be intermediates in a glycosyl transfer reaction. Glycosylation of the doublet requires a divalent cation, the effective ions being the same (except for Zn2+) as those that activate Golgi-localized β-glucan synthase (GS-I) activity. Treatments that inhibit GS-I also inhibit doublet glycosylation. The doublet is associated with Golgi (and to a minor extent with plasma) membranes and occurs also in the soluble fraction. The Golgi-bound doublet may be a component of the GS-I system. Immunological, inactivation, and fractionation evidence indicates that at least one other polypeptide is required in GS-I activity.
UR - http://www.scopus.com/inward/record.url?scp=0025721904&partnerID=8YFLogxK
M3 - Journal article
C2 - 1834664
AN - SCOPUS:0025721904
VL - 266
SP - 21977
EP - 21984
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 32
ER -
ID: 308328081