Identification and molecular characterization of the alternative spliced variants of beta carbonic anhydrase 1 (βCA1) from Arabidopsis thaliana

Jinyu Shen; Zhiyong Li; Yajuan Fu; Jiansheng Liang

doi:10.7717/peerj.12673

Identification and molecular characterization of the alternative spliced variants of beta carbonic anhydrase 1 (βCA1) from Arabidopsis thaliana

PeerJ. 2021 Dec 23:9:e12673. doi: 10.7717/peerj.12673. eCollection 2021.

Authors

Jinyu Shen^#¹, Zhiyong Li^#^{2

3}, Yajuan Fu¹, Jiansheng Liang^{1

3}

Affiliations

¹ Department of Biology, Southern University of Science and Technology, Shenzhen, China.
² Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Shenzhen, China.
³ Key Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Biology, Southern University of Science and Technology, Shenzhen, China.

^# Contributed equally.

Abstract

Carbonic anhydrases (CAs) are ubiquitous zinc metalloenzymes that catalyze the interconversion of carbon dioxide and bicarbonate. Higher plants mainly contain the three evolutionarily distinct CA families αCA, βCA, and γCA, with each represented by multiple isoforms. Alternative splicing (AS) of the CA transcripts is common. However, there is little information on the spliced variants of individual CA isoforms. In this study, we focused on the characterization of spliced variants of βCA1 from Arabidopsis. The expression patterns and subcellular localization of the individual spliced variants of βCA1 were examined. The results showed that the spliced variants of βCA1 possessed different subcellular and tissue distributions and responded differently to environmental stimuli. Additionally, we addressed the physiological role of βCA1 in heat stress response and its protein-protein interaction (PPI) network. Our results showed that βCA1 was regulated by heat stresses, and βca1 mutant was hypersensitive to heat stress, indicating a role for βCA1 in heat stress response. Furthermore, PPI network analysis revealed that βCA1 interacts with multiple proteins involved in several processes, including photosynthesis, metabolism, and the stress response, and these will provide new avenues for future investigations of βCA1.

Keywords: Carbonic anhydrase; Expression pattern; Localization; Protein-protein interaction network; Spliced variant; Stress response.

Grants and funding

The project was funded by the Key Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes (2019KSYS006) and the National Natural Science Foundation of China (31801277). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.