Characterization of a strong dominant phytochrome A mutation unique to phytochrome a signal propagation
Characterization of a strong dominant phytochrome A mutation unique to phytochrome a signal propagation
Here, we report the isolation and characterization of a strong dominant-negative phytochrome A(phyA) mutation (phyA-300D) in Arabidopsis. This mutation carries a single amino acid substitution at residue 631, from valine to methionine (V631M), in the core region within the C-terminal half of PHYA. This PHYA core region contains two protein-interactive motifs, PAS1 and PAS2. Val-631 is located within the PAS1 motif. The phyA-V631M mutant protein is photochemically active and accumulates to a level similar to wild type in dark-grown seedlings. Overexpression of PHYA-V631M in a wild-type background results in a dominant-negative interference with endogenous wild-type phyA, whereas PHYA-V631M in aphyA null mutant background is inactive. To investigate the specificity of this mutation within the phytochrome family, the corresponding amino acid substitution (V664M) was created in the PHYTOCHROME B (PHYB) polypeptide. We found that the phyB-V664M mutant protein is physiologically active in phyB mutant and causes no interfering effect in a wild-type background. Together, our results reveal a unique feature in phyA signal propagation through the C-terminal core region
457-465
Fry, Rebecca C.
288b601c-98c0-494e-8581-d255d7f05556
Habashi, Jessica
a4069c9b-8c9b-452f-8edd-930a22f00c18
Okamoto, Haruko
cea35380-7618-44c8-a268-47b0198cc7f9
Deng, Xing Wang
4e1d848e-08c4-43d2-8a79-c42b062b742f
2002
Fry, Rebecca C.
288b601c-98c0-494e-8581-d255d7f05556
Habashi, Jessica
a4069c9b-8c9b-452f-8edd-930a22f00c18
Okamoto, Haruko
cea35380-7618-44c8-a268-47b0198cc7f9
Deng, Xing Wang
4e1d848e-08c4-43d2-8a79-c42b062b742f
Fry, Rebecca C., Habashi, Jessica, Okamoto, Haruko and Deng, Xing Wang
(2002)
Characterization of a strong dominant phytochrome A mutation unique to phytochrome a signal propagation.
Plant Physiology, 130 (1), .
(10.?1104/?pp.?005264).
Abstract
Here, we report the isolation and characterization of a strong dominant-negative phytochrome A(phyA) mutation (phyA-300D) in Arabidopsis. This mutation carries a single amino acid substitution at residue 631, from valine to methionine (V631M), in the core region within the C-terminal half of PHYA. This PHYA core region contains two protein-interactive motifs, PAS1 and PAS2. Val-631 is located within the PAS1 motif. The phyA-V631M mutant protein is photochemically active and accumulates to a level similar to wild type in dark-grown seedlings. Overexpression of PHYA-V631M in a wild-type background results in a dominant-negative interference with endogenous wild-type phyA, whereas PHYA-V631M in aphyA null mutant background is inactive. To investigate the specificity of this mutation within the phytochrome family, the corresponding amino acid substitution (V664M) was created in the PHYTOCHROME B (PHYB) polypeptide. We found that the phyB-V664M mutant protein is physiologically active in phyB mutant and causes no interfering effect in a wild-type background. Together, our results reveal a unique feature in phyA signal propagation through the C-terminal core region
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Published date: 2002
Organisations:
Centre for Biological Sciences
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Local EPrints ID: 362185
URI: http://eprints.soton.ac.uk/id/eprint/362185
DOI: 10.?1104/?pp.?005264
ISSN: 0032-0889
PURE UUID: d9eb1d26-0333-458c-a877-6ac2375fa4a7
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Date deposited: 14 Mar 2014 14:08
Last modified: 14 Mar 2024 16:01
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Author:
Rebecca C. Fry
Author:
Jessica Habashi
Author:
Haruko Okamoto
Author:
Xing Wang Deng
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