7 research outputs found
Molecular evolution of plant beta-glucan endohydrolases
No full textPeter B. Høj and Geoffrey B. Finche
Active site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of 2 1,3-1,4-β-D-glucan 4-glucanohydrolases: the importance of epoxide stereochemistry for enzyme inactivation
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Grapevines for the new millennium - a research and development plan for grapevines for the next century
No full textConfocal measurement of the three-dimensional size and shape of plant parenchyma cells in developing fruit tissue
No full textGray, John D. ; Kolesik, Peter ; Høj, Peter B. ; And Coombe, Bryan G
Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase
No full textThe 90 kDa heat shock protein (HSP90) is an ATP-binding molecular chaperone with an associated ATPase activity having nucleoplasmin and HSP70-binding homology domains and containing Ca-binding EF-hands and a nuclear localization signal. Here we characterize the HSP90-associated ATPase and show that it is (i) a P-type ATPase inhibited by molybdate and vanadate, (ii) able to hydrolyze methylfluorescein phosphate with a 5–6-fold higher affinity, (iii) a 3-times better GTPase than ATPase in the presence of calcium and (iv) HSP27 and F-actin, but not HSP10 can “convert” the HSP90-associated ATPase activity to HSP90 autokinase activity. The HSP90-associated ATP/GTPase may participate in the regulation of complex formation of HSP90 with other proteins, such as F-actin, tubulin and heat shock proteins
