Comprehensive characterization of Guanosine monophosphate synthetase in Nicotiana tabacum
文献类型: 外文期刊
第一作者: Huang, Feiyan
作者: Huang, Feiyan;Yanguo, Ke;Yu, Lei;Abbas, Farhat;Fiaz, Sajid;Imran, Muhammad;Yanguo, Ke;Hassan, Waseem;Ashraf, Umair;He, Yuansheng;Cai, Xuanjie;Wang, Zhijiang;Ye, Xianwen;Chen, Xiaolong
作者机构:
关键词: Nicotiana tabacum; Guanosine monophosphate; In silico analysis; Tissue expression
期刊名称:MOLECULAR BIOLOGY REPORTS ( 影响因子:2.316; 五年影响因子:2.357 )
ISSN: 0301-4851
年卷期:
页码:
收录情况: SCI
摘要: Background Guanosine monophosphate (GMP) synthetase is an enzyme that converts xanthosine monophosphate to GMP. GMP plays an essential role in plant development and responses to internal and external stimuli. It also plays a crucial role in several plant physiochemical processes, such as stomata closure, cation flux regulation, pathogen responses and chloroplast development. Methods and results The mRNA sequences of NtGMP synthase in tobacco (Nicotiana tabacum) were rapidly amplified from cDNA. The GMP synthase open reading frame contains a 1617 bp sequence encoding 538 amino acids. A sequence analysis showed that this sequence shares high homology with that of Nicotiana sylvestris, Nicotiana attenuata, N. tomentosiformis, Solanum tuberosum, Lycopersicon pennellii, L. esculentum, Capsicum annuum, C. chinense and C. baccatum GMP synthase. A BLAST analysis with a tobacco high-throughput genomic sequence database revealed that the tobacco GMP synthase gene has five introns and six exons. A phylogenetic analysis showed a close genetic evolutionary relationship with N. sylvestris GMP synthase. The tissue-specific expression profile was evaluated using quantitative real-time PCR. The data showed that NtGMP synthase was highly expressed in leaves and moderately expressed in roots, flowers, and stems. The subcellular localization was predicted using the WOLF PSORT webserver, which strongly suggested that it might be localized to the cytoplasm. Conclusions In the current study, we cloned and comprehensively characterized GMP synthase in tobacco (Nicotiana tabacum). Our results establish a basis for further research to explore the precise role of this enzyme in tobacco.
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