Plant polypeptides reversibly glycosylated by UDP-glucose. Possible components of golgi β-glucan synthase in pea cells
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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.
Originalsprog | Engelsk |
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Tidsskrift | Journal of Biological Chemistry |
Vol/bind | 266 |
Udgave nummer | 32 |
Sider (fra-til) | 21977-21984 |
Antal sider | 8 |
ISSN | 0021-9258 |
Status | Udgivet - 1991 |
ID: 308328081