Tityustoxin K alpha blocks voltage-gatednoninactivating K+ channels and unblocks inactivating K+ channels blocked byalpha-dendrotoxin in synaptosomes.

Abstract

authors request that the sequence shown in Fig. 2 of the original report should be corrected as follows. As shown schematically here in Fig. 1 A, nucleotides 1452-1504 of the original report have to be replaced by a novel sequence shown here in Fig. 1B. This correction pertains to the 5Ј-flanking region of the gene and does not affect the coding region nor any of the conclusions drawn in the original report. The fact that there was a missing sequence element was discovered and pointed out to us by Tracy L. Bale in the laboratory of Daniel M. Dorsa, Departments of Psychiatry and Behavioral Sciences and Pharmacology, University of Washington, Seattle. As illustrated in Fig. 1 A, the novel sequence has to be inserted at the location of a dinucleotide repeat, (GT) 26 , located 89 nucleotides 5Ј to the main transcriptional initiation site. Resequencing of a newly generated phage subclone as well as Southern blot and PCR analyses (not shown) confirmed that the sequence presented here is indeed part of the genomic sequence. Since this novel sequence element is itself flanked by two dinucleotide repeats, (GT) 20 and (GT) 24 , respectively, a likely explanation is that this segment was spliced out during subcloning due to recombination between the two dinucleotide repeats. This idea is further supported by the fact that dinucleotide repeats that have the potential of forming Z-DNA structures have been shown to enhance recombination in extrachromosomal DNA up to 20-fold (1). Despite the recurrence of dinucleotide repeats around chromosomal rearrangement breakpoints, their role in mediating recombination on intact chromosomes remains, however, uncertain (2).We thank Tracy L. Bale and Daniel M. Dorsa for pointing out the error and for their help and collaboration in its correction. Fig. 3, A and C, are of (M ϩ 33H) 33ϩ .17. Mariman, E. C. M., Broers, C. A. M., Claesen, C. A.

Tityus Serrulatus Venom 1271‐29‐0

“…Finally, no significant similarity was found for some other isolated clones after DNA sequence analysis using GenBanK databases and the Fasta program of Pearson and Lipman (1988). In conclusion, we described the use of ELISA in the Comparison of amino acid sequence of cTsTxKb with BmTxKb2 (a putative potassium ion channel blocker from Buthus martensii, Zhu et al, 1999); TsTx-Kb (potassium ion channel blocker from Titus serrulatus, Rogowski et al, 1994) and clones Ts5 H Cl.14 and Ts3 H Cl.3 (Legros et al, 1998). Numbering corresponding to the signal peptide is negatively numbered.…”

“…Of interest is clone 64 called here cTsTx-Kb (cDNA of TsTx-Kb), whose deduced amino acid sequence (Fig. 3) showed 64% identity with the long chain potassium ion channel blocker BmTxKb2 isolated from the scorpion Buthus martensii (Zhu et al, 1999), approximately 91% with the toxin TsTx-Kb described by Rogowski et al (1994) and its sequence is almost identical to the partial sequence of clones Ts-5 H Cl.14 and Ts-3 H Cl.3 published by Legros et al (1998). However, a deletion of a guanine base at Comparison of amino acid sequence of TbTx5 with TbTx IV-5 and TsTx.…”

Adaptive Evolution after Gene Duplication in α-KT × 14 Subfamily from Buthus martensii Karsch

“…31 aa mature peptide of BmKK 14 had two disulfide bridge motif: Cys17-Ala-Arg-Lys-Cys21 and Cys28-Ala-Cys30 (Cysab), which played a great role for forming a high conserved 3D structure with one a-helix and two b-sheets (29). There are a lot of Pro amino acid residues in mature peptide of BmKK 14 , which possibly effected structure and function of BmKK 14 . BmKK 14 shareed high homology with BmKK 1 -3 and BmSKT 6 1 -2 at amino acid level including signal peptide and mature peptide, as shown in Fig.…”

“…There are a lot of Pro amino acid residues in mature peptide of BmKK 14 , which possibly effected structure and function of BmKK 14 . BmKK 14 shareed high homology with BmKK 1 -3 and BmSKT 6 1 -2 at amino acid level including signal peptide and mature peptide, as shown in Fig. 6.…”

“…1, 2, and 3 present the total scorpion DNA after HindIII, EcoRI, and PstI + ClaI digestion, respectively. sequencing primer and analyzed by PC Gene and Genbank Blast (GenBank: http://www.ncbi.nlm.nih.gov/BLAST), one of which was a full length scorpion cDNA sequence homology with BmKK 1 -3 and BmSKT 6 1 -2 genes (named BmKK 14 and GenBank number: AY730620). Sequence analysis showed that the full length BmKK 14 precursor nucleotide sequence was 304bp, including 53bp 5'UTR, 86bp 3'UTR and 165bp ORF (Open Reading Frame).…”