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פותח על ידי קלירמאש פתרונות בע"מ -
Pollination‐induced senescence in phalaenopsis petals. Relationship of ethylene sensitivity to activity of GTP‐binding proteins and protein phosphorylation
Year:
1994
Source of publication :
Physiologia Plantarum
Authors :
פורת, רון
;
.
Volume :
90
Co-Authors:
Porat, R., Kennedy-Leigh Center for Horticulture Research, Faculty of Agriculture, Hebrew Univ. of Jerusalem, P.O. Box 12, Rehovot, 76-100, Israel
Borochov, A., Kennedy-Leigh Center for Horticulture Research, Faculty of Agriculture, Hebrew Univ. of Jerusalem, P.O. Box 12, Rehovot, 76-100, Israel
Halevy, A.H., Kennedy-Leigh Center for Horticulture Research, Faculty of Agriculture, Hebrew Univ. of Jerusalem, P.O. Box 12, Rehovot, 76-100, Israel
Facilitators :
From page:
679
To page:
684
(
Total pages:
6
)
Abstract:
Treatments of cut phalaenopsis (Phalaenopsis hybrid, cv. ‘Herbert Hager’) flowers with cholera toxin or guanosine‐5‐0‐(3‐thiotriphosphate), compounds that modulate GTP‐binding protein activity, increased the sensitivity of the flowers to ethylene. Guanosine‐5‐0‐(2‐thiodiphosphate) which does not affect the activity of GTP‐binding proteins, had no affect on the sensitivity to ethylene. Western blot analysis of microsomal proteins, revealed that a peptide with a molecular mass of ca 42 kDa cross‐reacts with antibodies against a well‐conserved amino acid sequence (Gα‐commun peptide) of mammalian G‐proteins. Calcium ions, known co‐factors of protein kinases, also increased the sensitivity of the flowers to ethylene, while EGTA, a chelator of calcium, decreased it. Phorbol 12‐myrisate 13‐acetate, a phorbol ester, had no effect on the sensitivity to ethylene. Protein phosphorylation in petal microsomal membranes was doubled in the presence of calcium ions, but was unaffected by phorbol ester. Ten h after pollination, at the peak of ethylene sensitivity, a significant increase of ca 20% was measured in the binding of GTP to the membranes. Protein phosphorylation in flowers increased significantly following pollination, with a single peptide of ca 30 kDa most heavily phosphorylated. These observations may indicate a direct involvement of GTP‐binding proteins, and protein phosphorylation, two major components of the cellular signal transduction pathway, in the regulation of pollination induced ethylene sensitivity in phalaenopsis petals. Copyright © 1994, Wiley Blackwell. All rights reserved
Note:
Related Files :
ethylene
GTP‐binding proteins
Phalaenopsis hybrid
protein phospharylation
עוד תגיות
תוכן קשור
More details
DOI :
10.1111/j.1399-3054.1994.tb02523.x
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19436
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:29
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Scientific Publication
Pollination‐induced senescence in phalaenopsis petals. Relationship of ethylene sensitivity to activity of GTP‐binding proteins and protein phosphorylation
90
Porat, R., Kennedy-Leigh Center for Horticulture Research, Faculty of Agriculture, Hebrew Univ. of Jerusalem, P.O. Box 12, Rehovot, 76-100, Israel
Borochov, A., Kennedy-Leigh Center for Horticulture Research, Faculty of Agriculture, Hebrew Univ. of Jerusalem, P.O. Box 12, Rehovot, 76-100, Israel
Halevy, A.H., Kennedy-Leigh Center for Horticulture Research, Faculty of Agriculture, Hebrew Univ. of Jerusalem, P.O. Box 12, Rehovot, 76-100, Israel
Pollination‐induced senescence in phalaenopsis petals. Relationship of ethylene sensitivity to activity of GTP‐binding proteins and protein phosphorylation
Treatments of cut phalaenopsis (Phalaenopsis hybrid, cv. ‘Herbert Hager’) flowers with cholera toxin or guanosine‐5‐0‐(3‐thiotriphosphate), compounds that modulate GTP‐binding protein activity, increased the sensitivity of the flowers to ethylene. Guanosine‐5‐0‐(2‐thiodiphosphate) which does not affect the activity of GTP‐binding proteins, had no affect on the sensitivity to ethylene. Western blot analysis of microsomal proteins, revealed that a peptide with a molecular mass of ca 42 kDa cross‐reacts with antibodies against a well‐conserved amino acid sequence (Gα‐commun peptide) of mammalian G‐proteins. Calcium ions, known co‐factors of protein kinases, also increased the sensitivity of the flowers to ethylene, while EGTA, a chelator of calcium, decreased it. Phorbol 12‐myrisate 13‐acetate, a phorbol ester, had no effect on the sensitivity to ethylene. Protein phosphorylation in petal microsomal membranes was doubled in the presence of calcium ions, but was unaffected by phorbol ester. Ten h after pollination, at the peak of ethylene sensitivity, a significant increase of ca 20% was measured in the binding of GTP to the membranes. Protein phosphorylation in flowers increased significantly following pollination, with a single peptide of ca 30 kDa most heavily phosphorylated. These observations may indicate a direct involvement of GTP‐binding proteins, and protein phosphorylation, two major components of the cellular signal transduction pathway, in the regulation of pollination induced ethylene sensitivity in phalaenopsis petals. Copyright © 1994, Wiley Blackwell. All rights reserved
Scientific Publication
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