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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Bibliographic Details
Published in:The Plant journal : for cell and molecular biology 1993, Vol.4 (2), p.399-402
Main Authors: Clark, G. B., Memon, A. R., Thompson, G. A. Jr, Roux, S. J.
Format: Article
Language:English
Subjects:
Cell Nucleus - metabolism
GTP-Binding Proteins - metabolism
GTP-Binding Proteins - physiology
Life Sciences (General)
Light
Phosphorus Radioisotopes
Phytochrome - metabolism
Pisum sativum - cytology
Pisum sativum - metabolism
Signal Transduction - physiology
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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.
ISSN:0960-7412
1365-313X
DOI:10.1046/j.1365-313X.1993.04020399.x