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대두 Bowman - Birk trypsin isoinhibitor PI Ⅳ의 cDNA 유전자 분리
안중훈,김희진,최양도,김수일 ( Joohg Hoon Ahn,Hee Jin Kim,Yang Do Choi,Su Il Kim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2
Three different kinds of proteinase inhibitors are known in soybeans; Kunitz trypsin inhibitor, Bowman-Birk trypsin inhibitor (BBTI) and its isoinhibitors. A cDNA clone for the soybean trypsin inhibitor was isolated from a soybean λgt11 cDNA library by plaque hybridization with a oligonucleotide probe which corresponds to the N-terminal region of the BBTI. The cDNA clone λB13 was 446bp long and the nucleotide sequencing reveals that there were one open reading frame of 243 bp, the 5` leader sequences of 70 bp and the 3`-untranslating region of 133 bp in the cDNA clone λB13. Nucleotide sequences at the 5` and 3` noncoding regions were highly homologous, respectively, to those of the BBTI and isoinhibitor C-2. Compared the deduced amino acid sequences to the amino acid sequences of proteinase inhibitor, it corresponds to the Bowman-Birk trypsin isoinhibitor PI IV. Sequences around the reactive site of Arg-Ser were repeated twice, giving the double headed structure. Northern blot analysis demonstrated that the size of the mRNA was about 700 nucleotides. It was expressed only in soybean seed maintaining tissue specific gene expression pattern. Expression level was increased with the maturation of seed and reached maximum in full size seed. It suggests that the expression of the isoinhibitor PI IV could be regulated at the transcriptional level.
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