CAJ | 학술논문

通过火炬松等松属树种的cDNA序列同源克隆了湿地松的左旋β－蒎烯合成酶基因（ PeTPS－（－） BPin），分析表明该基因与其他松属植物之间的同源性在90％以上，与松科其他属植物之间的同源性在80％以上。裸子植物不同萜烯合成酶基因（ TPS）之间的同源性在70％以上。被子植物与裸子植物的TPS基因亲缘关系较远。左旋β－蒎烯合成酶的蛋白质分子式为C3197H4972N862O957S32，分子量为71．74 ku，带弱正电，为不稳定蛋白，易分解，含37个磷酸化位点，定位在叶绿体。蛋白质二级结构含有4个不规则卷曲，24个α－螺旋，三级结构中含有一个cd00684保守域。 ELM中找到7个可能的功能域，包括一个NDR切割位点、两个磷酸肽配体、一个PDZ配体、一个SH2配体、两个磷酸化位点。在68、69位存在一个RR保守结构，猜测能够在第二个R的N末端断裂并与底物结合，从而参与底物异构化。在380～384位出现了DDxxD保守域，但未能在该区搜到可能的功能位点。预测的两个磷酸化位点位于302、623位氨基酸。
통과화거송등송속수충적cDNA서렬동원극륭료습지송적좌선β－파희합성매기인（ PeTPS－（－） BPin），분석표명해기인여기타송속식물지간적동원성재90％이상，여송과기타속식물지간적동원성재80％이상。라자식물불동첩희합성매기인（ TPS）지간적동원성재70％이상。피자식물여라자식물적TPS기인친연관계교원。좌선β－파희합성매적단백질분자식위C3197H4972N862O957S32，분자량위71．74 ku，대약정전，위불은정단백，역분해，함37개린산화위점，정위재협록체。단백질이급결구함유4개불규칙권곡，24개α－라선，삼급결구중함유일개cd00684보수역。 ELM중조도7개가능적공능역，포괄일개NDR절할위점、량개린산태배체、일개PDZ배체、일개SH2배체、량개린산화위점。재68、69위존재일개RR보수결구，시측능구재제이개R적N말단단렬병여저물결합，종이삼여저물이구화。재380～384위출현료DDxxD보수역，단미능재해구수도가능적공능위점。예측적량개린산화위점위우302、623위안기산。
The sinistral beta pinene synthetase gene ( PeTPS?(?) BPin) was isolated from Pinus elliottii by the cDNA sequence of pinus such as loblolly pine. Sequence analysis indicated that the deduced protein se?quence of the PeTPS?(?) BPin shared 90% and 80 % of identity with the other Pinus and the other genera of pinaceae,respectively.And the similarities of the sequence with different TPS genes of gymnosperms were 70%,which had distant relationship to angiosperm.The PeTPS?(?)BPin in Pinus elliottii was labile,with a molecular weight of 71.74 ku,phosphorylation site 37,locating in the chloroplasts. There were 4 poikilo?coils and 24 α?helixes on biomolecular structures,and a cd00684 conserved domain on tertiary structure.Seven potential func?tional domains were searched in ELM,including a NDR cleavage site,two phosphopeptide ligands,a PDZ lig?and,a SH2 ligand and two Phosphorylation sites,respectively.ARR conservative domain existed in the 68 and 69 amino acid,it was surmised that the N?terminal on the second R of the RR conservative domain broke,and was combined with the substrates,which participated in the isomerization of the substrates.The DDxxD conser?vative domains appeared but the potential functional site could not be found in the 380~384 amino acid. The two predicted phosphorylation sites located at 302 and 623 amino acid.