Phytochrome regulates GTP-binding protein activity in the envelope of pea nuclei
Three GTP-binding proteins with apparent molecular masses of 27, 28 and 30 kDa have been detected in isolated nuclei of etiolated pea plumules. After LDS-PAGE and transfer to nitrocellulose these proteins bind [32P]GTP in the presence of excess ATP, suggesting that they are monomeric G proteins. Whe...
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Published in | The Plant journal : for cell and molecular biology Vol. 4; no. 2; pp. 399 - 402 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Headquarters
Blackwell Science Ltd
1993
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Subjects | |
Online Access | Get full text |
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Summary: | Three GTP-binding proteins with apparent molecular masses of 27, 28 and 30 kDa have been detected in isolated nuclei of etiolated pea plumules. After LDS-PAGE and transfer to nitrocellulose these proteins bind [32P]GTP in the presence of excess ATP, suggesting that they are monomeric G proteins. When nuclei are disrupted, three proteins co-purify with the nuclear envelope fraction and are highly enriched in this fraction. The level of [32P]GTP-binding for all three protein bands is significantly increased when harvested pea plumules are irradiated by red light, and this effect is reversed by far-red light. The results indicate that GTP-binding activity associated with the nuclear envelope of plant cells is photoreversibly regulated by the pigment phytochrome. |
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Bibliography: | HQ Headquarters ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0960-7412 1365-313X |
DOI: | 10.1046/j.1365-313X.1993.04020399.x |