CAJ | 학술논문

ε亚基是叶绿体ATP合酶最小的一个亚基,有阻塞ATP合酶的质子通道和抑制其水解ATP活力的两种功能.用定点突变和缺失等分子生物学方法对ε亚基的结构功能进行了研究,结果表明:ε亚基42位上的苏氨酸(Thr42)对维持其结构和功能都很重要.与大肠杆菌ATP合酶相比,叶绿体ATP合酶ε亚基C端和N端的氨基酸残基缺失对其结构功能的影响更为敏感.
ε아기시협록체ATP합매최소적일개아기,유조새ATP합매적질자통도화억제기수해ATP활력적량충공능.용정점돌변화결실등분자생물학방법대ε아기적결구공능진행료연구,결과표명:ε아기42위상적소안산(Thr42)대유지기결구화공능도흔중요.여대장간균ATP합매상비,협록체ATP합매ε아기C단화N단적안기산잔기결실대기결구공능적영향경위민감.
The ε-subunit is the smallest subunit of chloroplast ATP synthase, and is known to inhibitATPase activity in isolated CF1-ATPase. As a result ε is sometimes called an inhibitory subunit. In addition,and perhaps more importantly, the ε-subunit is essential for the coupling of proton translocation to ATPsynthesis (as proton gate). The relation between the structure and function of ε-subunit of ATP synthasein higher plant chloroplast has been studied by molecular biological methods such as site-directed mu-tagenesis and truncations for C- or N-terminus of ε-subunit. The results showed that: (1) Thr42 of ε-subunit is important for its structure and function; (2) compared with the ε-subunit in E.coli, the ε-subunitof chloroplast ATP synthase is more sensitive to C- or N-terminus truncations.