2010•Zhongnan Linye Keji Daxue xuebaoRequires access

Cloning and sequence analysis of full-length cDNAs encoding oleosins from Vernicia fordii

Jiao Hu

Open publisher page 5 citations

Abstract

The oleosin of Vernicia fordii is closely related to the storage of fatty acid.Two full length cDNAs of oleosin gene were isolated and cloned from developing seeds of V.fordii by the cDNA library and EST library-based molecular techniques.The two full length cDNAs were 738 bp and 838 bp.They contained a complete CDS(coding sequence) of 738 bp and 838 bp encoding 137 amino acids and 154 amino acids,respectively.They were named VF_ole Ⅰand VF_ole Ⅱ.Amino acid sequence aligenment with 19 oleosins from other species showed that the two oleosins of V.fordii displayed the highest similarity(90.3%,88.3%) to R.communis oleosin and J.curcas oleosin 2.The predicted isoelectric points of the two V.fordii oleosins were 10.315 and 10.335.A membrane spanning domain was present in the two genes.There was a large possibility of the existence of cleavage site for signal peptide with a long hydrophobic region in the central sequence and α-helix in C-terminal.

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The oleosin of Vernicia fordii is closely related to the storage of fatty acid.Two full length cDNAs of oleosin gene were isolated and cloned from developing seeds of V.fordii by the cDNA library and EST library-based molecular techniques.The two full length cDNAs were 738 bp and 838 bp.They contained a complete CDS(coding sequence) of 738 bp and 838 bp encoding 137 amino acids and 154 amino acids,respectively.They were named VF_ole Ⅰand VF_ole Ⅱ.Amino acid sequence aligenment with 19 oleosins from other species showed that the two oleosins of V.fordii displayed the highest similarity(90.3%,88.3%) to R.communis oleosin and J.curcas oleosin 2.The predicted isoelectric points of the two V.fordii oleosins were 10.315 and 10.335.A membrane spanning domain was present in the two genes.There was a large possibility of the existence of cleavage site for signal peptide with a long hydrophobic region in the central sequence and α-helix in C-terminal.

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Available abstract

The oleosin of Vernicia fordii is closely related to the storage of fatty acid.Two full length cDNAs of oleosin gene were isolated and cloned from developing seeds of V.fordii by the cDNA library and EST library-based molecular techniques.The two full length cDNAs were 738 bp and 838 bp.They contained a complete CDS(coding sequence) of 738 bp and 838 bp encoding 137 amino acids and 154 amino acids,respectively.They were named VF_ole Ⅰand VF_ole Ⅱ.Amino acid sequence aligenment with 19 oleosins from other species showed that the two oleosins of V.fordii displayed the highest similarity(90.3%,88.3%) to R.communis oleosin and J.curcas oleosin 2.The predicted isoelectric points of the two V.fordii oleosins were 10.315 and 10.335.A membrane spanning domain was present in the two genes.There was a large possibility of the existence of cleavage site for signal peptide with a long hydrophobic region in the central sequence and α-helix in C-terminal.

Key concepts: Oleosin, Signal peptide, Biology, Amino acid, Coding region, Complementary DNA, Peptide sequence, cDNA library

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