Functional analysis of N-terminal domains of Arabidopsis chlorophyllide a oxygenase

Sakuraba Yasuhito; Yamasato Akihiro; Tanaka Ryouichi; Tanaka Ayumi

Title	en Functional analysis of N-terminal domains of Arabidopsis chlorophyllide a oxygenase
Creator	en Sakuraba, Yasuhito en Yamasato, Akihiro en Tanaka, Ryouichi NRID 1000020311516 en Tanaka, Ayumi NRID 1000010197402
Accessrights	open access
Subject	Other en Chlorophyllide a oxygenase Other en Chlorophyll cycle Other en Arabidopsis NDC 471
Description	Abstract en Higher plants acclimate to various light environments by changing the antenna size of a light harvesting photosystem. The antenna size of a photosystem is partly determined by the amount of chlorophyll b in the light-harvesting complexes. Chlorophyllide a oxygenase (CAO) converts chlorophyll a to chlorophyll b in a two-step oxygenation reaction. In our previous study, we demonstrated that the cellular level of the CAO protein controls accumulation of chlorophyll b. We found that the amino acids sequences of CAO in higher plants consist of three domains (A, B, and C domains). The C domain exhibits a catalytic function, and we demonstrated that the combination of the A and B domains regulates the cellular level of CAO. However, the individual function of each of A and B domain has not been determined yet. Therefore, in the present study we constructed a series of deleted CAO sequences that were fused with green fluorescent protein and overexpressed in a chlorophyll b-less mutant of Arabidopsis thaliana, ch1-1, to further dissect functions of A and B domains. Subsequent comparative analyses of the transgenic plants overexpressing B-domain containing proteins and those lacking the B domain determined that there was no significant difference in CAO protein levels. These results indicate that the B domain is not involved in the regulation of the CAO protein levels. Taken together, we concluded that the A domain alone is involved in the regulatory mechanism of the CAO protein levels.
Publisher	en Elsevier
Date	Issued2007-10
Language	eng
Resource Type	journal article
Version Type	AM
Identifier	HDL http://hdl.handle.net/2115/33905
Relation	URI http://www.sciencedirect.com/science/journal/09819428 isVersionOf DOI https://doi.org/10.1016/j.plaphy.2007.07.016 PMID 17884554
Journal	PISSN 0981-9428 en Plant Physiology and Biochemistry Volume Number45 Issue Number10-11 Page Start740 Page End749
File	fulltext tanaka2.pdf 1.09 MB (application/pdf) Issued2007-10
Oaidate	2023-07-26