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Bulletin of Botanical Research ›› 2018, Vol. 38 ›› Issue (4): 543-550.doi: 10.7525/j.issn.1673-5102.2018.04.008

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Bioinformatic Analysis of Serine Hydroxymethyltransferase(SHMT) Gene in Bletilla striata

SHEN Fang1,2, LI Lin2, PAN Yin-Chi2, ZHANG She-Bo2, MA Ji2, XU De-Lin2   

  1. 1. Affiliated Hospital of Zunyi Medical University, Zunyi 563000;
    2. Department of Cell Biology, Zunyi Medical University, Zunyi 563099
  • Received:2017-12-27 Online:2018-07-15 Published:2018-07-21
  • Supported by:
    Nation Natural Science Foundation of China(31560079,31560087);Science and technology research project of Guizhou(黔科合LH字[2014]7549号);The Research and Development of The Modernization of Traditionnal Chinese Medicine in GuiZhou Province(黔科合ZY字[2013]3002号);The "15851" talent engineering project of ZunYi city 2014(201424);Elite talent engineering project of Zunyi Medical University

Abstract: Serine hydroxymethyl transferase(SHMT) is a key enzyme in the processes of one-carbon metabolism and photosynthesis. Exploring its sequence information through bioinformatics analyzing could comprehensively peep at the protein structure and functions. We picked out the SHMT sequence(NCBI accession ID:MG544187) from the transcriptome of Bletilla striata(Thunb.) Rchb. f., and then applied a series of tools to explore the biological information of this gene. We detected that this gene has 1 953 bp in length and coding 471 amino acid residues, which sharing the highest similarity with the SHMT gene of Dendrobium catenatum as 93%. The protein had a predicted molecular weight of 51.861 06 kD and theoretical isoelectric point of 7.17. According to the protein's secondary structure, we revealed it shared several highly conserved domains with other species' SHMT genes. And its tertiary was a homo-tetramer structure without transmembrane components and signal peptide but contained several phosphorylation sites. Through the subcellular localization analysis, this protein was mainly located in cytoplasm and Chloroplast. This analysis lays a solid foundation for future studies on SHMT's function confirming, mechanism revelation and application for genetically improving in B.striata. This study also provides some basic data for studies on SHMT genes of other species.

Key words: Bletilla striata, serine hydroxymethyl transferase, sequence analysis, structure prediction

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