Chlorophyll-Protein Complexes of a Photosystem II Mutant of Maize : Evidence that Chlorophyll-Protein a-2 and a Chlorophyll-Protein Complex Derived from a Photosystem I Antennae System Comigrate on Polyacrylamide Gels

Abstract

Use of the octyl beta-d-glucopyranoside solubilization procedure of Camm and Green (1980 Plant Physiol 66: 428-432) reveals that thylakoid membranes of a photosystem (PS) II-deficient maize (Zea mays L.) mutant lack two chlorophyll protein (CP) complexes associated with PSII, i.e. CPa-1 and CPa-2. In contrast, when lithium dodecyl sulfate is used to solubilize the membranes of the mutant prior to electrophoretic separation, a CP complex is observed which has a mobility similar to that of CPa-2. Comparison of spectral characteristics and polypeptide composition of the green bands in this region taken from samples of the mutant, normal sibling control plants and from PSII preparations indicate that the CP complex observed in the mutant represents a portion of a light-harvesting complex of PSI (Mullet et al. 1980 Plant Physiol 65: 814-822). The green band observed in normal maize samples can contain both the CPa-2 complex as well as the CP complex derived from the PSI antennae system.