J
Jindong Zhao
Researcher at Chinese Academy of Sciences
Publications - 66
Citations - 2326
Jindong Zhao is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Heterocyst & Phycobilisome. The author has an hindex of 24, co-authored 53 publications receiving 1910 citations. Previous affiliations of Jindong Zhao include Peking University.
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Journal ArticleDOI
Genome-wide ORFeome cloning and analysis of Arabidopsis transcription factor genes.
Wei Gong,Yunping Shen,Ligeng Ma,Yi Pan,Yun-Long Du,Dong-Hui Wang,Jian-Yu Yang,Li-De Hu,Xin-Fang Liu,Chun-Xia Dong,Li Ma,Yanhui Chen,Xiaoyuan Yang,Ying Gao,Danmeng Zhu,Xiaoli Tan,Jin-Ye Mu,Dabing Zhang,Yule Liu,Savithramma P. Dinesh-Kumar,Yi Li,Xiping Wang,Hongya Gu,Li-Jia Qu,Shu-Nong Bai,Ying-Tang Lu,Jiayang Li,Jindong Zhao,Jianru Zuo,Hai Huang,Xing Wang Deng,Yu-Xian Zhu +31 more
TL;DR: Novel alternative splicing of TF gene transcripts is responsible for the observed differences in at least five genes, however, thoseAlternative splicing events do not appear to be differentially regulated among distinct Arabidopsis tissues examined.
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Structure of phycobilisome from the red alga Griffithsia pacifica
TL;DR: The structure of a 16.8-megadalton PBS from a red alga at 3.5 Å resolution obtained by single-particle cryo-electron microscopy is reported, revealing the mechanisms underlying specific interactions between linkers and phycobiliproteins, and the formation of linker skeletons.
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HetR homodimer is a DNA-binding protein required for heterocyst differentiation, and the DNA-binding activity is inhibited by PatS
TL;DR: It is presented evidence that shows that the up-regulation of patS and hetR depends on DNA binding by HetR dimer, and the pentapeptide RGSGR, which is present at the C terminus of PatS and blocks heterocyst formation, inhibits the DNA binding of HtR and prevents het R up- regulation.
Journal ArticleDOI
Assembly of photosystem I. I. Inactivation of the rubA gene encoding a membrane-associated rubredoxin in the cyanobacterium Synechococcus sp. PCC 7002 causes a loss of photosystem I activity.
Gaozhong Shen,Jindong Zhao,Susan K. Reimer,Mikhail L. Antonkine,Qun Cai,Sharon M. Weiland,John H. Golbeck,Donald A. Bryant +7 more
TL;DR: The results indicate that RubA plays a specific role in the biogenesis of PS I, and overproduction of the water-soluble rubredoxin domain inEscherichia coli led to a product with the absorption and EPR spectra of typical rubredoxins.
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Structural organization of an intact phycobilisome and its association with photosystem II
TL;DR: The results provide insights into the molecular architecture of an intact PBS at different assembly levels and provide the basis for understanding how the light energy absorbed by PBS is transferred to PSII.