Munn A L, Whitfeld P R, Bottomley W, Hudson G S, Jans D A, Gibson F, Cox G B
Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra City.
Biochim Biophys Acta. 1991 Sep 27;1060(1):82-8. doi: 10.1016/s0005-2728(05)80122-7.
The effect of the expression of the chloroplast F1-ATPase beta-subunit in two Escherichia coli beta-subunit mutant strains was investigated. The amount of chloroplast beta-subunit formed in E. coli was increased by introducing a 'Shine-Dalgarno' sequence upstream from the translation start site. The chloroplast beta-subunit was membrane bound but was unable to functionally replace the mutant beta-subunit in a strain carrying the uncD409 allele [corrected]. However, in an E. coli mutant strain unable to form the beta- and epsilon-subunits the presence of the chloroplast beta-subunit enabled the assembly of a functional proton pore [corrected]
研究了叶绿体F1 - ATP酶β亚基在两种大肠杆菌β亚基突变菌株中的表达效果。通过在翻译起始位点上游引入一个“Shine - Dalgarno”序列，增加了大肠杆菌中形成的叶绿体β亚基的量。叶绿体β亚基与膜结合，但在携带uncD409等位基因（已校正）的菌株中无法在功能上替代突变的β亚基。然而，在无法形成β亚基和ε亚基的大肠杆菌突变菌株中，叶绿体β亚基的存在使得能够组装一个功能性的质子孔（已校正）
