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 '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. 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.