Heterologous overexpression of the cyanobacterial alcohol dehydrogenase sysr1 confers cold tolerance to the oleaginous alga Nannochloropsis salina

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Title
Heterologous overexpression of the cyanobacterial alcohol dehydrogenase sysr1 confers cold tolerance to the oleaginous alga Nannochloropsis salina
Author(s)
Jong Min Lim; Sokyong Jung; Jae-Sun In; Y I Park; Won Joong Jeong
Bibliographic Citation
Frontiers in Plant Science, vol. 14, pp. 1045917-1045917
Publication Year
2023
Abstract
Temperature is an important regulator of growth in algae and other photosynthetic organisms. Temperatures above or below the optimal growth temperature could cause oxidative stress to algae through accumulation of oxidizing compounds such as reactive oxygen species (ROS). Thus, algal temperature stress tolerance could be attained by enhancing oxidative stress resistance. In plants, alcohol dehydrogenase (ADH) has been implicated in cold stress tolerance, eliciting a signal for the synthesis of antioxidant enzymes that counteract oxidative damage associated with several abiotic stresses. Little is known whether temperature stress could be alleviated by ADH in algae. Here, we generated transgenic lines of the unicellular oleaginous alga Nannochloropsis salina that heterologously expressed sysr1, which encodes ADH in the cyanobacterium Synechocystis sp. PCC 6906. To drive sysr1 expression, the heat shock protein 70 (HSP70) promoter isolated from N. salina was used, as its transcript levels were significantly increased under either cold or heat stress growth conditions. When subjected to cold stress, transgenic N. salina cells were more cold-tolerant than wild-type cells, showing less ROS production but increased activity of antioxidant enzymes such as superoxide dismutase, ascorbate peroxidase, and catalase. Thus, we suggest that reinforcement of alcohol metabolism could be a target for genetic manipulation to endow algae with cold temperature stress tolerance.
Keyword
Tolerance to temperature stressReactive oxygen species (ROS)Antioxidant enzymesAlcohol dehydrogenaseNannochloropsis salina
ISSN
1664-462X
Publisher
Frontiers Media Sa
Full Text Link
http://dx.doi.org/10.3389/fpls.2023.1045917
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Cell Factory Research Center > 1. Journal Articles
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