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Cloning and Characterization of a Novel cDNA Sequence Encoding the Precursor of a Novel Venom Peptide (BmKbpp) Related to a Bradykinin‐Potentiating Peptide from Chinese Scorpion Buthus martensii Karsch

Xian‐Chun Zeng, Wenxin Li, Fang Peng, Zhi‐Hui Zhu

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Abstract

Based on the amino acid sequence of a bradykinin-potentiating peptide (Bpp) (peptide K-12) from scorpion Buthus occitanus, a full-length cDNA sequence encoding the precursor of a novel venom peptide (named BmKbpp) related to this Bpp, has been isolated and analyzed. The cDNA encodes a precursor of 72 amino acid residues, including a signal peptide of 22 residues and an extra Arg-Arg-Arg tail at the C-terminal end of the precursor, which have to be removed in the processing step. The C-terminal region (21 residues) of the precursor is homologous (57% identical) with the sequence of peptide K-12. Thus, according to the primary structure of the BmKbpp precursor, there may be a propeptide between the signal peptide and the putative mature BmKbpp at the C-terminal region of the precursor.

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What this paper is about

Based on the amino acid sequence of a bradykinin-potentiating peptide (Bpp) (peptide K-12) from scorpion Buthus occitanus, a full-length cDNA sequence encoding the precursor of a novel venom peptide (named BmKbpp) related to this Bpp, has been isolated and analyzed. The cDNA encodes a precursor of 72 amino acid residues, including a signal peptide of 22 residues and an extra Arg-Arg-Arg tail at the C-terminal end of the precursor, which have to be removed in the processing step. The C-terminal region (21 residues) of the precursor is homologous (57% identical) with the sequence of peptide K-12. Thus, according to the primary structure of the BmKbpp precursor, there may be a propeptide between the signal peptide and the putative mature BmKbpp at the C-terminal region of the precursor.

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Available abstract

Based on the amino acid sequence of a bradykinin-potentiating peptide (Bpp) (peptide K-12) from scorpion Buthus occitanus, a full-length cDNA sequence encoding the precursor of a novel venom peptide (named BmKbpp) related to this Bpp, has been isolated and analyzed. The cDNA encodes a precursor of 72 amino acid residues, including a signal peptide of 22 residues and an extra Arg-Arg-Arg tail at the C-terminal end of the precursor, which have to be removed in the processing step. The C-terminal region (21 residues) of the precursor is homologous (57% identical) with the sequence of peptide K-12. Thus, according to the primary structure of the BmKbpp precursor, there may be a propeptide between the signal peptide and the putative mature BmKbpp at the C-terminal region of the precursor.

Key concepts: Peptide, Signal peptide, Complementary DNA, Peptide sequence, Venom, Biochemistry, Amino acid, Molecular biology

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Cloning and Characterization of a Novel cDNA Sequence Encoding the Precursor of a Novel Venom Peptide (BmKbpp) Related to a Bradykinin‐Potentiating Peptide from Chinese Scorpion Buthus martensii Karsch — Research Paper | ScholarLens