Affiliations
- School of Life Sciences, Anhui Agricultural University, 130 West Changjiang Road, Hefei 230036, China.
- Institute of Sericulture, Anhui Academy of Agricultural Sciences, 15 Huoshan Road, Hefei 230061, China.
- Anhui International Joint Research and Development Center of Sericulture Resources Utilization, Hefei 230036, China.
- Guangxi Zhuang Autonomous Region Research Academy of Sericultural Science, 10 Xiajun Road, Nanning 530007, China.
PMID: 32806497 PMCID: PMC7469206 DOI: 10.3390/insects11080523
Abstract
The most common type of RNA editing in metazoans is the deamination of adenosine into inosine (A-to-I) catalyzed by the adenosine deaminase acting on the RNA (ADAR) family of proteins. The deletion or dysfunction of ADAR enzymes in higher eukaryotes can affect the efficiency of substrate editing and cause neurological disorders. However, the information concerning A-to-I RNA editing and ADAR members in the silkworm, Bombyx mori (BmADAR), is limited.
In this study, a first molecular comprehensive cloning and sequence analysis of BmADAR transcripts was presented. A complete open reading frame (ORF) (BmADARa) was obtained using RT-PCR and RACE and its expression pattern, subcellular localization and A-to-I RNA-editing function on the silkworm synaptotagmin I (BmSyt I) were investigated. Subcellular localization analysis observed that BmADARa was mainly localized in the nucleus.
To further study the A-to-I RNA-editing function of BmADARa, BmSyt I-pIZ-EGFP was constructed and co-transfected with BmADARa-pIZ-EGFP into BmN cells. The result demonstrates that BmADARa can functionally edit the specific site of BmSyt I. Taken together, this study not only provides insight into the function of the first ADAR enzyme in B. mori, but also lays foundations for further exploration of the functional domain of BmADARa and its editing substrates and target sites.
Keywords: A-to-I RNA editing; Bombyx mori; adenosine deaminase; subcellular localization; synaptotagmin I.
