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作 者:陈鹏吉 李国泽 邵亚林 李雪[1] 赵平[2] 陆燕元 丁勇[1] Chen Pengji;Li Guoze;Shao Yalin;Li Xue;Zhao Ping;Lu Yanyuan;Ding Yong(Key Laboratory of Forest Biotechnology in Yunnan,Southwest Forestry University,Kunming,650224;Key Laboratory of State Forestry and Grassland Administration on Highly-Efficient Utilization of Forestry Biomass Resources in Southwest China,Southwest Forestry University,Kunming,650224;College of Forestry,Southwest Forestry University,Kunming,650224)
机构地区:[1]西南林业大学,云南省高校林木生物技术重点实验室,昆明650224 [2]西南林业大学,西南地区林业生物质资源高效利用国家林业与草原局重点实验室,昆明650224 [3]西南林业大学林学院,昆明650224
出 处:《分子植物育种》2021年第8期2527-2537,共11页Molecular Plant Breeding
基 金:国家自然科学基金项目(31960073,31460076);云南省高校林木生物技术重点实验室开放基金(51700201);植物化学与西部植物资源持续利用国家重点实验室开放基金(P2017-KF10)共同资助。
摘 要:作为植物抗氧化防御系统的主要保护酶之一,过氧化氢酶在植物细胞响应逆境胁迫应答方面发挥重要作用。本研究通过生物信息学分析RNA-Seq数据(NCBI登录号:PRJNA285946),结合RT-PCR技术首次从樟叶越桔成熟叶片中获得了过氧化氢酶基因VdCAT1全长为1 611 bp的cDNA序列,完整开放阅读框(ORF)长度为1 479 bp;推测编码的VdCAT1蛋白含492个氨基酸,相对分子量为56.96 kD,理论等电点(pI)为6.65,总平均疏水系数为-0.545;推测VdCAT1为无跨膜结构域、非分泌性亲水蛋白质。VdCAT1二级结构主要由随机卷曲和α-螺旋等构件组成。樟叶越桔VdCAT1基因编码的氨基酸序列与茶树CsCAT1和拟南芥AtCAT1等过氧化氢酶氨基酸序列具有较高的同源性和较近的亲缘关系。本研究结果为日后揭示VdCAT1基因的生理学功能及其表达调控机制提供科学依据。As one of the main protective enzymes in the plant’s antioxidant defense system, catalase plays an important role in plant cells in response to stress. In this study, the gene VdCAT1 with a full-length cDNA comprised 1 611 nucleotides was primordial obtained by bioinformatics analysis of RNA-Seq data(NCBI registration number: PRJNA285946) and RT-PCR amplification from Vaccinium dunalianum Wight. The results showed that the open reading frame(ORF) of VdCAT1 gene was 1 479 bp, encoding VdCAT1 protein of 492 amino acids. The molecular weight of the VdCAT1 protein was 56.96 kD, the isoelectric point(pI) was 6.65 and the total mean hydrophobic coefficient was-0.545. It was speculated that VdCAT1 was a non-secretory hydrophilic protein without transmembrane domain. The main parts of predicted secondary structures of VdCAT1 protein were random coils and alpha helix. VdCAT1 protein encoded by gene VdCAT1 from V. dunalianum shared high homology and close relationship with CsCAT1 protein from Camellia sinensis and AtCAT1 protein from Arabidopsis thaliana. The study provides scientific basis for revealing the physiological function and expression regulation mechanism of VdCAT1 gene.
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