2014Nonwood Forest ResearchRequires access

Cloning and sequence analysis of full-length cDNA of accA subunit in Vernicia fordii

Zhanhui Wang

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Abstract

In order to reveal sequence features and structural function of accA gene in Vernicia fordii, and to lay a foundation for further research, development and utilization, taking nearly ripe seeds in V. fordii as materials, the specifi c primers were designed according to the results of transcriptome sequencing analysis of V. fordii, and full-length cDNA sequences of accA gene were cloned by RT-PCR technique. The results show that full-length cDNA sequence of accA gene is 2 313 bp, encoding 770 amino acids. Iso electric point(pI) of accA protein is 8.48, the relative molecular mass is 85 902.7 Da, and the stability coeffi cient is 37.33. The results of bioinformatics analysis show that, the protein has four obvious trans-membrane domains, and is an unstable non-secretory protein. The results of motif research show that a Carboxyl transferase domain and a ACCA functional domain are located in α subunit. The tertiary structure of this protein has 14 α helixes, and appears a spherical body with a extended part. The gene has been submitted to the GeneBank and named by VfCTα.

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What this paper is about

In order to reveal sequence features and structural function of accA gene in Vernicia fordii, and to lay a foundation for further research, development and utilization, taking nearly ripe seeds in V. fordii as materials, the specifi c primers were designed according to the results of transcriptome sequencing analysis of V. fordii, and full-length cDNA sequences of accA gene were cloned by RT-PCR technique. The results show that full-length cDNA sequence of accA gene is 2 313 bp, encoding 770 amino acids. Iso electric point(pI) of accA protein is 8.48, the relative molecular mass is 85 902.7 Da, and the stability coeffi cient is 37.33. The results of bioinformatics analysis show that, the protein has four obvious trans-membrane domains, and is an unstable non-secretory protein. The results of motif research show that a Carboxyl transferase domain and a ACCA functional domain are located in α subunit. The tertiary structure of this protein has 14 α helixes, and appears a spherical body with a extended part. The gene has been submitted to the GeneBank and named by VfCTα.

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Available abstract

In order to reveal sequence features and structural function of accA gene in Vernicia fordii, and to lay a foundation for further research, development and utilization, taking nearly ripe seeds in V. fordii as materials, the specifi c primers were designed according to the results of transcriptome sequencing analysis of V. fordii, and full-length cDNA sequences of accA gene were cloned by RT-PCR technique. The results show that full-length cDNA sequence of accA gene is 2 313 bp, encoding 770 amino acids. Iso electric point(pI) of accA protein is 8.48, the relative molecular mass is 85 902.7 Da, and the stability coeffi cient is 37.33. The results of bioinformatics analysis show that, the protein has four obvious trans-membrane domains, and is an unstable non-secretory protein. The results of motif research show that a Carboxyl transferase domain and a ACCA functional domain are located in α subunit. The tertiary structure of this protein has 14 α helixes, and appears a spherical body with a extended part. The gene has been submitted to the GeneBank and named by VfCTα.

Key concepts: Complementary DNA, Biology, Gene, Sequence analysis, Cloning (programming), Protein subunit, cDNA library, Protein sequencing

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