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Cloning and Genomic Characterization of a Natural Insecticidal Peptide LaIT1 with Unique DDH Structural Fold
Author(s) -
Chen Jing,
Xu Yue,
San Mingkui,
Cao Zhijian,
Li Wenxin,
Wu Yingliang,
Chen Zongyun
Publication year - 2015
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21686
Subject(s) - peptide , gene , genomic dna , exon , biology , intron , genetics , biochemistry , microbiology and biotechnology , chemistry
ABSTRACT Two native peptides with disulfide‐directed hairpin (DDH) fold, LaIT1 and LITX, were recently isolated from scorpion venom, a development that offered insights into exploring the evolutionary linkage between DDH and inhibitor cystine knot (ICK) peptides. In this work, we isolated and identified the full‐length cDNAs of LaTI1, a representative member with DDH fold, and further determined its complete gene structure. The precursor organization of LaIT1 is similar to that of ICK peptides. The LaIT1 gene contains four exons interrupted by three unique introns and differed from ICK peptides, suggesting divergent genomic organizations of DDH peptides and ICK peptides. Phylogenetic analysis further showed that the “simple” DDH peptide originates from the “complex” ICK peptide, rather than the reverse. To the best of our knowledge, this is the first report on the genomic organization of DDH‐fold peptides, and it presents new evidence of an evolutionary linkage between ICK and DDH peptides.