Plastids were isolated from a plastome mutator-induced mutant (pm7) of Oenothera hookeri and were analyzed for various physiological and biochemical attributes. No photosynthetic electron transport activity was detected in the mutant plastids. This is consistent with previous ultrastructural analysis showing the absence of thylakoid membranes in the pm7 plastids and with the observation of aberrant processing and accumulation of chloroplast proteins in the mutant. In comparison to wild type, the mutant tissue lacks chlorophyll, and has significant differences in levels of four fatty acids. The analyses did not reveal any differences in carotenoid levels nor in the synthesis of several chloroplast lipids. The consequences of the altered composition of the chloroplast membrane are discussed in terms of their relation to the aberrant protein processing of the pm7 plastids. The pigment, fatty acid, and lipid measurements were also performed on two distinct nuclear genotypes (A/A and A/C) which differ in their compatibility with the plastid genome (type 1) contained in these lines. In these cases, only chlorophyll concentrations differed significantly.A large number of plastome (or plastid genome) mutants have been generated through the use of the plastome mutator system in the Johansen strain of Oenothera hookeri (15). The mutants thus far accumulated in this collection display various degrees ofchlorosis as well as differing extents ofaberrant chloroplast development as seen at the ultrastructural level (13,14). Immunological analysis of plastid proteins from one of these plastome mutants, pm7, has provided evidence that indicates the existence of a defect in chloroplast protein processing (EM Johnson, BB Sears, L Schnabelrauch, unpublished data). Proteins affected include one encoded by a chloroplast gene (Cytf) as well as the 16-and 23-kD subunits of the oxygen evolving complex of PSII, which are nuclear gene products. The suggestion that the processing of these three proteins in pm7 may be inhibited by a lesion of some shared feature of the proteolytic machinery is