HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Institute of Low Temperature Science >
Peer-reviewed Journal Articles, etc >

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

Files in This Item:
tanaka2.pdf1.11 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/33905

Title: Functional analysis of N-terminal domains of Arabidopsis chlorophyllide a oxygenase
Authors: Sakuraba, Yasuhito Browse this author
Yamasato, Akihiro Browse this author
Tanaka, Ryouichi Browse this author →KAKEN DB
Tanaka, Ayumi Browse this author →KAKEN DB
Keywords: Chlorophyllide a oxygenase
Chlorophyll cycle
Arabidopsis
Issue Date: Oct-2007
Publisher: Elsevier
Journal Title: Plant Physiology and Biochemistry
Volume: 45
Issue: 10-11
Start Page: 740
End Page: 749
Publisher DOI: 10.1016/j.plaphy.2007.07.016
PMID: 17884554
Abstract: 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.
Relation: http://www.sciencedirect.com/science/journal/09819428
Type: article (author version)
URI: http://hdl.handle.net/2115/33905
Appears in Collections:低温科学研究所 (Institute of Low Temperature Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田中 亮一

Export metadata:

OAI-PMH ( junii2 , jpcoar )


 

Feedback - Hokkaido University