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Chloroplasts are believed to be descendants of ancestral cyanobacteria that have a peptidoglycan layer between the outer and the inner membranes. In particular, cyanelles having peptidoglycan in Cyanophora paradoxa are considered as evidence for the endosymbiotic origin of chloroplasts. The moss Physcomitrella patens has a complete set of genes involved in the synthesis of peptidoglycan, but a peptidoglycan layer has not been observed by conventional electron microscopy to date. Recently, a new metabolic labeling technique using a fluorescent probe was applied to visualize putative peptidoglycan surrounding the chloroplasts. The exact localization of the peptidoglycan, however, has not been clearly identified. Here we examined conventional electron micrographs of two types of moss materials (mutants or ampicillin-treated plants), one presumably having peptidoglycan and the other presumably lacking peptidoglycan, and analyzed in detail, by single-pixel densitometry, the electron density of the chloroplast envelope membranes and the intermembrane space. Statistical analysis showed that the relative electron density within the intermembrane space with respect to that of the envelope membranes was significantly higher in the materials presumably having peptidoglycan than in the materials presumably devoid of peptidoglycan. We consider this difference as bona fide evidence for the presence of peptidoglycan between the outer and the inner envelope membranes in the wild-type chloroplasts of the moss, although its density is lower than that in bacteria and cyanelles. We will also discuss this low-density peptidoglycan in the light of the phylogenetic origin of peptidoglycan biosynthesis enzymes., (© The Author 2017. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oup.com.)

Algae are smaller organisms than land plants and offer clear advantages in research over terrestrial species in terms of rapid production, short generation time and varied commercial applications. Thus, studies investigating the practical development of effective algal production are important and will improve our understanding of both aquatic and terrestrial plants. In this study we estimated multiple physicochemical and secondary structural properties of protein sequences, the predicted presence of post-translational modification (PTM) sites, and subcellular localization using a total of 510,123 protein sequences from the proteomes of 31 algal and three plant species. Algal species were broadly selected from green and red algae, glaucophytes, oomycetes, diatoms and other microalgal groups. The results were deposited in the Algal Protein Annotation Suite database (Alga-PrAS; http://alga-pras.riken.jp/), which can be freely accessed online., (© The Author 2017. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists.)

The supercomplex organization of photosystem complexes was studied in various cyanobacteria, a glaucocystophyte and a primitive rhodophyte by blue-native PAGE with a wide range of detergent concentrations. In contrast to known cyanobacteria that produced the PSI trimer, a filamentous N(2)-fixing cyanobacterium Anabaena sp. PCC 7120 and a glaucocystophyte Cyanophora paradoxa NIES 547 had a PSI tetramer and dimer but no trimer at all. This was confirmed by sucrose density gradient centrifugation. A primitive rhodophyte Cyanidioschyzon merolae had two species of PSI monomeric complex with a light-harvesting Chl complex of a different composition. These results are discussed with regard to the evolution of the PSI supercomplex.

Novel eukaryotic chlorophyll-carotenoid proteins have evolved at least twice following the origin of the plastid and include the widely distributed integral membrane light-harvesting complexes (LHCs) and the dinoflagellate-specific soluble peridinin-chlorophyll proteins. In the glaucophytes, homologs of these proteins are reportedly absent. We have identified a novel carotenoid-rich protein (CRP) in the glaucophyte Cyanophora paradoxa that is 28 kDa and immunologically related to the family of LHCs. CRP is associated with the thylakoid membrane, though it can be removed by stringent washes, suggesting that there are probably significant structural differences between CRP and the LHCs. CRP co-localizes with a zeaxanthin-rich thylakoid membrane fraction that also contains beta-carotene, chlorophyll and an unidentified carotenoid. Despite this, we found no evidence for carotenoid-chlorophyll energy transfer in the isolated complex, suggesting that light harvesting may not be a primary function. The presence of CRP in C. paradoxa is evidence for the evolution of a novel pigment-binding protein in the glaucophytes.