The β-amylase PbrBAM3 from pear (Pyrus betulaefolia) regulates soluble sugar accumulation and ROS homeostasis in response to cold stress. (October 2019)
- Record Type:
- Journal Article
- Title:
- The β-amylase PbrBAM3 from pear (Pyrus betulaefolia) regulates soluble sugar accumulation and ROS homeostasis in response to cold stress. (October 2019)
- Main Title:
- The β-amylase PbrBAM3 from pear (Pyrus betulaefolia) regulates soluble sugar accumulation and ROS homeostasis in response to cold stress
- Authors:
- Zhao, Liangyi
Yang, Tianyuan
Xing, Caihua
Dong, Huizheng
Qi, Kaijie
Gao, Junzhi
Tao, Shutian
Wu, Juyou
Wu, Jun
Zhang, Shaoling
Huang, Xiaosan - Abstract:
- Highlights: Subcellular localization assay indicates that PbrBAM3 is located in chloroplast. PbrBAM3 was responsive to various types of abiotic stresses, particularly cold. Transgenic tobacco and pear overexpressing PbrBAM3 showed better cold tolerance. Abstract: β -Amylase (BAM) is involved in sugar metabolism, but the role of BAM genes in cold tolerance remains poorly understood. Here, we report the identification and functional characterization of the chloroplast-localized BAM-encoding gene PbrBAM3 isolated from Pyrus betulaefolia . The transcript levels of PbrBAM3 were up-regulated under cold, dehydration and ABA, but repressed by maltose. Overexpression of PbrBAM3 in tobacco (Nicotiana tabacum ) and pear ( P. ussuriensis ) conferred increased BAM activity, promoted starch degradation after chilling treatments and enhanced tolerance to cold. Under the chilling stress, the transgenic tobacco and P. ussuriensis exhibited lessened reactive oxygen species (ROS) generation, higher levels of antioxidant enzymes activity, and greater accumulation of soluble sugars (specially maltose) than the corresponding wild type plants. Taken together, these results demonstrate that PbrBAM3 plays an important role in cold tolerance, at least in part, by raising the levels of soluble sugars capable of acting as osmolytes or antioxidants.
- Is Part Of:
- Plant science. Volume 287(2019)
- Journal:
- Plant science
- Issue:
- Volume 287(2019)
- Issue Display:
- Volume 287, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 287
- Issue:
- 2019
- Issue Sort Value:
- 2019-0287-2019-0000
- Page Start:
- Page End:
- Publication Date:
- 2019-10
- Subjects:
- Cold stress -- β-amylase (BAM) -- Osmolyte -- Starch degradation -- Antioxidant enzyme -- Reactive oxygen species (ROS)
Botany -- Periodicals
Botanique -- Périodiques
580 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01689452 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.plantsci.2019.110184 ↗
- Languages:
- English
- ISSNs:
- 0168-9452
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6523.390000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 14211.xml