2010•Journal of Harbin University of CommerceRequires access

Cloning and bioinformatics analysis of LVAP1 gene and product protein in leymus chinensis

Yin Yue-yia

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Abstract

To clone the VHA-c gene in leymus chinensis and predict structure and function of its product protein.Amplify cDNA from the total RNA of leymus chinensis by RACE technology and predict protein structure and function by bioinformatics methods.Obtains the LVAP1 gene(GenBank accession number GQ397276) from leaves of leymus chinensis,the opening reading-frame(ORF) of this gene is 498 bp and encoding 165 amino acid.This protein is composed of four putative α helix transmembrane domains.The Glu142,a highly conserved residue in the fourth putative transmembrane domain,is possible binding sites of protons.Phylogenetic tree analysis of VHA-c shows LVAP1 of leymus chinensis is highly identified with VHA-c in triticum aestivum,suaeda salsa and mesembryanthemum crystallinum,could presume that they have the similar biological functions.

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What this paper is about

To clone the VHA-c gene in leymus chinensis and predict structure and function of its product protein.Amplify cDNA from the total RNA of leymus chinensis by RACE technology and predict protein structure and function by bioinformatics methods.Obtains the LVAP1 gene(GenBank accession number GQ397276) from leaves of leymus chinensis,the opening reading-frame(ORF) of this gene is 498 bp and encoding 165 amino acid.This protein is composed of four putative α helix transmembrane domains.The Glu142,a highly conserved residue in the fourth putative transmembrane domain,is possible binding sites of protons.Phylogenetic tree analysis of VHA-c shows LVAP1 of leymus chinensis is highly identified with VHA-c in triticum aestivum,suaeda salsa and mesembryanthemum crystallinum,could presume that they have the similar biological functions.

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Available abstract

To clone the VHA-c gene in leymus chinensis and predict structure and function of its product protein.Amplify cDNA from the total RNA of leymus chinensis by RACE technology and predict protein structure and function by bioinformatics methods.Obtains the LVAP1 gene(GenBank accession number GQ397276) from leaves of leymus chinensis,the opening reading-frame(ORF) of this gene is 498 bp and encoding 165 amino acid.This protein is composed of four putative α helix transmembrane domains.The Glu142,a highly conserved residue in the fourth putative transmembrane domain,is possible binding sites of protons.Phylogenetic tree analysis of VHA-c shows LVAP1 of leymus chinensis is highly identified with VHA-c in triticum aestivum,suaeda salsa and mesembryanthemum crystallinum,could presume that they have the similar biological functions.

Key concepts: Leymus, GenBank, Gene, Open reading frame, Biology, Genetics, Complementary DNA, Hypothetical protein

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