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Phytochrome regulates GTP‐binding protein activity in the envelope of pea nuclei
Author(s) -
Clark Gregory B.,
Memon Abdul R.,
Tong ChiiGong,
Thompson Guy A.,
Roux Stanley J.
Publication year - 1993
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1993.04020399.x
Subject(s) - gtp' , etiolation , phytochrome , biochemistry , biophysics , g protein , biology , chemistry , microbiology and biotechnology , botany , red light , receptor , enzyme
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 [ 32 p]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 [ 32 P]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.