Precursor nucleotide sequence and genomic organization of BmTXKS1, a new scorpion toxin-like peptide from Buthus martensii Karsch.

  title={Precursor nucleotide sequence and genomic organization of BmTXKS1, a new scorpion toxin-like peptide from Buthus martensii Karsch.},
  author={S Y Zhu and W X Li and X. C. Zeng},
  journal={Toxicon : official journal of the International Society on Toxinology},
  volume={39 9},
  • S. ZhuW. LiX. Zeng
  • Published 1 September 2001
  • Biology, Chemistry
  • Toxicon : official journal of the International Society on Toxinology

Molecular cloning, genomic organization and functional characterization of a new short‐chain potassium channel toxin‐like peptide BmTxKS4 from Buthus martensii Karsch(BmK)

Taken together, BmTxKS4 is a novel subfamily member of short‐strain K+‐channel scorpion toxin, which can modulate Na+, K+, Cl−, and Ca2+ ion–channel conductance in the cell membrane.

Two non-coding transcripts of toxins from the scorpion Buthus martensii Karsch: Evidence for the existence of NMD in scorpion venom gland cells

Analysis of nucleotide sequences shows that their 5′ sequences are identical to the 5t’UTR and upstream open reading frame (ORF) sequences of the cDNAs encoding BmαTX15 and BmTXK β, two toxins from Buthus martensii Karsch, providing evidence for the existence of nonsense-mediated mRNA decay (NMD) pathway in scorpion venom gland cells.

The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition

Small cationic antimicrobial peptides (SCAMPs) as effectors of animal innate immunity provide the first defense against infectious pathogens. This class of molecules exists widely in invertebrate

An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch.

Overview of Scorpion Species from China and Their Toxins

The bridge between scorpion species and their toxins is built, which helps to understand the molecular and functional diversity of scorpion venom arsenal, the dynamic and functional evolution of scorpio toxins, and the potential relationships of scorpions species andTheir toxins.

Splicing of scorpion toxin gene BmKK2 in HEK 293T cells

The results suggested that introns of scorpion toxin genes BmKK2 and BmP03 increase the diversity of scorpions toxins and regulate the expression of their genes.



Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels.

Four peptidyl inhibitors of the small-conductance Ca2+-activated K+ channels (SK(Ca) channels) have been isolated from the venom of the Chinese scorpion Buthus martensi by means of mass analysis by matrix-assisted-laser-desorption/ionization time-of-flight mass spectrometry, and toxicological tests in mice.

Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1H-NMR structure of leiuropeptide II.

To extend the knowledge about the structural features of short scorpion toxins, the ion-exchange fractions obtained from Leiurus quinquestriatus hebraeus venom were investigated by plasma desorption mass spectrometry in order to select low molecular mass polypeptides that were devoid of any significant toxicity against mammals and insects.

Promoter structure and intron-exon organization of a scorpion alpha-toxin gene.

Analysis of DNA curvature by computer modeling revealed a strong bending centered around the transcription initiation site of the gene, in agreement with the previously reported correlation between DNA bending and promoter function.

Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels.

Three novel toxins belonging to the scorpion K+ channel-inhibitor family were purified to homogeneity from the venom of the Chinese scorpion Buthus martensi and should prove to be useful probes for studying the diverse family of K+ channels.

The Precursors of the Bee Venom Constituents Apamin and MCD Peptide Are Encoded by Two Genes in Tandem Which Share the Same 3′-Exon (*)

It is proposed that the mRNA encoding the apamin precursor originates from a primary transcript which starts in the third intron of the MCD peptide gene, which contains a putative TATA box.

Chemical synthesis and structure-activity relationships of Ts kappa, a novel scorpion toxin acting on apamin-sensitive SK channel.

Data from binding assay, together with conformational analysis of the synthetic analogues by 1H-NMR, suggest that Arg6, and to a lesser extent Arg9, are important residues for an high-affinity interaction of this toxin with SK channels; interestingly these residues are located outside thealpha-helical structure, whereas the pharmacologically important basic residues from other SK channel-specific toxins had been located inside the alpha-helix.