Gatenby A A, Rothstein S J
Gene. 1986;41(2-3):241-7. doi: 10.1016/0378-1119(86)90104-6.
The maize chloroplast gene for the beta subunit (atpB) of the chloroplast CF1 component of ATPase from maize, when fused to either the lacZ or ral genes in the vectors pMC1403 or pHUB4, is expressed in Escherichia coli as a fusion protein with beta-galactosidase or with bacteriophage lambda Ral sequences. Some of the fusion proteins are converted to a membrane-bound form, as determined by differential and sucrose-gradient centrifugation. The specificity of membrane binding has been examined using E. coli unc mutants that are defective in binding of the F1 ATPase component to the F0 receptor site on the membrane, and by the use of two different length maize atpB::lacZ gene fusions. We show that the first 365 N-terminal amino acids (aa) of the maize beta subunit are involved in binding to the E. coli inner membrane, and that this binding is probably mediated by the bacterial F0 receptor.
玉米叶绿体ATP酶CF1组分β亚基（atpB）的叶绿体基因，当与载体pMC1403或pHUB4中的lacZ或ral基因融合时，在大肠杆菌中作为与β-半乳糖苷酶或与噬菌体λ Ral序列的融合蛋白表达。通过差速离心和蔗糖梯度离心测定，一些融合蛋白转化为膜结合形式。利用在F1 ATP酶组分与膜上F0受体位点结合方面存在缺陷的大肠杆菌unc突变体，以及使用两种不同长度的玉米atpB::lacZ基因融合体，研究了膜结合的特异性。我们表明，玉米β亚基的前365个N端氨基酸参与与大肠杆菌内膜的结合，并且这种结合可能由细菌F0受体介导。
