scholarly journals Functional characterization of ent-copalyl diphosphate synthase, kaurene synthase and kaurene oxidase in the Salvia miltiorrhiza gibberellin biosynthetic pathway

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Ping Su ◽  
Yuru Tong ◽  
Qiqing Cheng ◽  
Yating Hu ◽  
Meng Zhang ◽  
...  
2018 ◽  
Vol 40 (7) ◽  
Author(s):  
Yanyan Jia ◽  
Jingling Liu ◽  
Zhenqing Bai ◽  
Kai Ding ◽  
Hongyan Li ◽  
...  

2021 ◽  
Vol 12 ◽  
Author(s):  
Min Jiang ◽  
Fen Zhang ◽  
Qiao Yuan ◽  
Peixing Lin ◽  
Hao Zheng ◽  
...  

Carotenoids are organic pigments that play an important role in both plant coloration and human health; they are a critical subject in molecular breeding due to growing demand for natural molecules in both food and medicine. In this study, we focus upon characterizing BoaCRTISO, the carotenoid isomerase gene before the branch of the carotenoid biosynthetic pathway, which is expressed in all organs and developmental stages of Chinese kale, and BoaCRTISO, which is located in the chloroplast. The expression of BoaCRTISO is induced by strong light, red and blue combined light, and gibberellic acid treatment, but it is suppressed by darkness and abscisic acid treatment. We obtained BoaCRTISO-silenced plants via virus-induced gene silencing technology, and the silence efficiencies ranged from 52 to 77%. The expressions of most carotenoid and chlorophyll biosynthetic genes in BoaCRTISO-silenced plants were downregulated, and the contents of carotenoids and chlorophyll were reduced. Meanwhile, BoaCRTISO-silenced plants exhibited phenotypes of yellowing leaves and inhibited growth. This functional characterization of BoaCRTISO provides insight for the biosynthesis and regulation of carotenoid in Chinese kale.


PLoS ONE ◽  
2013 ◽  
Vol 8 (9) ◽  
pp. e73259 ◽  
Author(s):  
Shuncang Zhang ◽  
Pengda Ma ◽  
Dongfeng Yang ◽  
Wenjing Li ◽  
Zongsuo Liang ◽  
...  

2003 ◽  
Vol 132 (1) ◽  
pp. 372-380 ◽  
Author(s):  
Hirotaka Uefuji ◽  
Shinjiro Ogita ◽  
Yube Yamaguchi ◽  
Nozomu Koizumi ◽  
Hiroshi Sano

2003 ◽  
Vol 185 (24) ◽  
pp. 7193-7201 ◽  
Author(s):  
Jesse D. Woodson ◽  
Carmen L. Zayas ◽  
Jorge C. Escalante-Semerena

ABSTRACT The ability of archaea to salvage cobinamide has been under question because archaeal genomes lack orthologs to the bacterial nucleoside triphosphate:5′-deoxycobinamide kinase enzyme (cobU in Salmonella enterica). The latter activity is required for cobinamide salvaging in bacteria. This paper reports evidence that archaea salvage cobinamide from the environment by using a pathway different from the one used by bacteria. These studies demanded the functional characterization of two genes whose putative function had been annotated based solely on their homology to the bacterial genes encoding adenosylcobyric acid and adenosylcobinamide-phosphate synthases (cbiP and cbiB, respectively) of S. enterica. A cbiP mutant strain of the archaeon Halobacterium sp. strain NRC-1 was auxotrophic for adenosylcobyric acid, a known intermediate of the de novo cobamide biosynthesis pathway, but efficiently salvaged cobinamide from the environment, suggesting the existence of a salvaging pathway in this archaeon. A cbiB mutant strain of Halobacterium was auxotrophic for adenosylcobinamide-GDP, a known de novo intermediate, and did not salvage cobinamide. The results of the nutritional analyses of the cbiP and cbiB mutants suggested that the entry point for cobinamide salvaging is adenosylcobyric acid. The data are consistent with a salvaging pathway for cobinamide in which an amidohydrolase enzyme cleaves off the aminopropanol moiety of adenosylcobinamide to yield adenosylcobyric acid, which is converted by the adenosylcobinamide-phosphate synthase enzyme to adenosylcobinamide-phosphate, a known intermediate of the de novo biosynthetic pathway. The existence of an adenosylcobinamide amidohydrolase enzyme would explain the lack of an adenosylcobinamide kinase in archaea.


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