A survey of isolated thylakoids from 11 different higher plant species (Spinacia oleracea L., Pisum sativum L., Vicia faba L., Brassica napus L., Vigna sinensis L., Vinca minor L., Secale cereale L., Triticum aestivum L., Triticosecale Wittn., Hordeum vulgare L., Zea mays L.) indicated that the ratio of the oligomeric:monomeric form of the light-harvesting complex 11 was twofold higher for the dicots (3.16 ± 0.35) than the monocots (1.64 ± 0.25) examined under identical separation procedures. Under conditions specifically designed to stabilize the oligomeric form in vitro, we show that the oligomeric form of dicot light-harvesting complex 11 is twice as stable to solubilization in the presence of sodium dodecyl sulfate (SDS) than that observed for monocots. This decreased stability of monocot light-harvesting complex 11 is associated with a twofold increase in the trienoic fatty acid level of thylakoid phosphatidylglycerol but with no significant changes in the trienoic fatty acid levels in the major galactolipids. In addition, SDS polyacrylamide gel electrophoresis and western blot analyses with monoclonal antibodies indicated that monocots exhibited greater heterogeneity in the polypeptide complements associated with subtractions of light-harvesting complex 11 than the dicots examined. The data indicate that the oligomeric form of the lightharvesting complex 11 is not the result of a simple oligomerization of a common monomeric unit. We suggest that the difference in stability of the oligomeric form of light-harvesting complex 11 in isolated thylakoids of monocots and dicots is probably due to a differential accessibility to SDS. The differential SDS accessibility may be due to differences in thylakoid protein-protein and/or protein-lipid interactions.The major Chl a/b LHCII2 was one of the first pigment proteins to be characterized in higher plants (6,26,27 Approximately 50% of Chl and about 30% of the protein present in higher plant thylakoids is associated with LHCII (25, 26). The remainder of the Chl is associated with LHCI, core antennae, and reaction center complexes of PSII and PSI (10, 22). The oligomeric form (LHCIIb) of LHCII, with an apparent molecular mass of 72 kD and a Chl a/b of 1.0 to 1.3, is considered to be the primary form of this complex. Upon denaturation of the holocomplex with SDS, typically three to four polypeptides are observed in the molecular mass range of 25 to 30 kD. These polypeptides are the products of a family of light-regulated, nuclear-encoded cab genes (6, 11).Although the in situ form of LHCIIb is not known for certain, recent crystallographic (17, 18) and biochemical data indicate that LHCIIb most likely exists as a trimeric structure. Freeze-fracture data for thylakoid membranes indicate that the 80A particle identified as LHCIIb may be a higher oligomer than the proposed trimer (25). Kuhlbrandt and Wang (18) have shown by electron crystallography at 6A resolution that three membrane-spanning a helices (A, B, and C) exist within the LHCIIb trimer to which 15 Chl...