Molecular Characterization of Ethylene Response Sensor 1 (BoERS1) in Bambusa oldhamii
| Autor: | Rita P.-Y. Chen, Chien-Chih Yang, Choun-Sea Lin, Bing-Yu Chiang, Ai-Yu Wang, Yi-Lin Hsieh, Ching-Fang Lu, Shu-Chien Liao |
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| Rok vydání: | 2015 |
| Předmět: |
0106 biological sciences
0301 basic medicine chemistry.chemical_classification biology Kinase cDNA library Histidine kinase Plant Science Bambusa oldhamii biology.organism_classification 01 natural sciences Molecular biology Amino acid 03 medical and health sciences Open reading frame 030104 developmental biology chemistry Biochemistry Phosphorylation Molecular Biology Histidine 010606 plant biology & botany |
| Zdroj: | Plant Molecular Biology Reporter. 34:387-398 |
| ISSN: | 1572-9818 0735-9640 |
| Popis: | An ethylene receptor gene named BoERS1 was cloned from a bamboo (Bambusa oldhamii) cDNA library. The open reading frame of BoERS1 was 1,899 bp and encoded a 632-amino acid protein, which contains the five conserved motifs (H, N, G1, F, and G2 boxes) of the bacterial two-component system histidine kinases and shows high sequence similarity with other ethylene receptors in plants, such as rice and maize. Expression of BoERS1 in bamboo shoots increased with the growth of the emerging shoots. In an in vitro kinase assay, the expressed histidine kinase domain of BoERS1 (BHK) was phosphorylated in the presence of Mn2+, and LC-ESI-MS/MS analysis showed that four amino acids, namely T442, S444, S489, and S503, were phosphorylated. It is interesting to note that S489 and S503 are located in a loop region (L1) that is found only in plant histidine kinase-containing enzymes. The identification of multiple phosphorylation sites on BoERS1 provides a new avenue for future structure–function studies of the ethylene receptor protein family. |
| Databáze: | OpenAIRE |
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