A yeast genomic library in the bacteriophage expression vector lambda gt11 was screened with a polyclonal anti-holo-ATPase antiserum resulting in the isolation of 54 immunoreactive clones. Four of these phage clones express in bacteria a polypeptide antigenically related to an 18 kDa subunit (P18) of the yeast mitochondrial ATPase complex. Molecular analysis of the yeast DNA inserts in these phage clones revealed two classes of yeast DNA that share little homology at the nucleotide sequence level and therefore may represent distinct separate genes. The polypeptides potentially encoded by these yeast DNA segments do show scattered short blocks of strong amino acid sequence homology, which may underlie the observed immunochemical relatedness between the proteins expressed in bacteria.