SUMMARYSeptins are a group of GTP-binding proteins that are multi-functional, with a well-known role in cytokinesis in animals and fungi. Although the functions of septins have been thoroughly studied in opisthokonts (fungi and animals), the function and evolution of plant/algal septins are not as well characterized. Here we describe septin localization and expression in the green algae Nannochloris bacillaris and Marvania geminata. The present data suggest that septins localize at the division site when cytokinesis occurs. In addition, we show that septin homologs may be found only in green algae, but not in other major plant lineages, such as land plants, red algae and glaucophytes. We also found other septin homolog-possessing organisms among the diatoms, Rhizaria and cryptomonad/haptophyte lineages. Our study reveals the potential role of algal septins in cytokinesis and/or cell elongation, and confirms that septin genes appear to have been lost in the Plantae lineage, except in some green algae.
SummaryIn plants, the prokaryote-derived chloroplast division protein FtsZ is divided into the FtsZ1 and FtsZ2 families. To clarify the relationship between FtsZ1 and FtsZ2 expression and chloroplast division in the unicellular green alga Nannochloris bacillaris, we compared FtsZ1 and FtsZ2 expression in alga cultured in 2 nutritionally different media. Cells grown in a rich medium had 1 FtsZ ring throughout the cell division cycle, whereas cells in an inorganic medium showed only 1 FtsZ ring during the chloroplast division phase. Both FtsZ1 and FtsZ2 mRNA levels in the rich medium were higher than those in the inorganic medium. However, a much larger difference in the amount of transcripts between cells cultured in the rich and in the inorganic media was observed in FtsZ2 than that in FtsZ1, suggesting different gene regulatory mechanisms between the FtsZ genes. N. bacillaris cells cultured in inorganic medium showed cell division photoperiodicity, whereas cells cultured in organic media proliferated continuously under a light/dark cycle. Although FtsZ1 was expressed constantly throughout the chloroplast division cycle in the rich medium, the increase in FtsZ1 mRNA level was simultaneous with chloroplast division under a light/dark cycle in the inorganic medium. FtsZ2 was expressed constantly in both media. The control of chloroplast division by regulating FtsZ ring formation is discussed.
Peridinin-containing dinoflagellates have small circular DNA molecules called minicircle DNAs, each of which encodes one, or occasionally a few, plastid proteins or ribosomal RNA. Dinoflagellate minicircle DNA is composed of two parts: a gene-coding sequence and a non-coding sequence that consists of several variable and core regions. The core regions are identical among the minicircle DNAs with different genes within a species or strain. Because such structure is very different from those of well known plastid DNAs, many functional and evolutionary questions have been raised for the minicircle DNAs, and several studies that focus on answering those questions are underway. However, the localization of minicircle DNA is still controversial: several lines of indirect evidence have implied plastid localization, whereas the nuclear localization of minicircle DNA has also been suggested in a species. In order to understand the evolution and function of minicircle DNA, it is important to know its precise localization. In this study, we sequenced two typical minicircle DNAs, one encodes psbA and the other encodes 23S rRNA genes, from an Amphidinium massartii strain (TM16). To determine the subcellular localization of these minicircle DNAs, we performed DNA-targeted whole cell fluorescence in situ hybridization with A. massartii minicircle DNA-specific probes and demonstrated that minicircle DNAs were present in plastids. This study provides the first direct evidence for the plastid localization of dinoflagellate minicircle DNAs.
Chloroplasts of the unicellular green alga Nannochloris bacillaris Naumann cultured under nutrient-enriched conditions have multiple rings of FtsZ, a prokaryote-derived chloroplast division protein. We previously reported that synthesis of excess chloroplast DNA and formation of multiple FtsZ rings occur simultaneously. To clarify the role of multiple FtsZ rings in chloroplast division, we investigated chloroplast DNA synthesis and ring formation in cells cultured under various culture conditions. Cells transferred from a nutrient-enriched medium to an inorganic medium in the light showed a drop in cell division rate, a reduction in chloroplast DNA content, and changes in the shape of chloroplast nucleoids as cells divided. We then examined DNA synthesis by immunodetecting BrdU incorporated into DNA strands using the anti-BrdU antibody. BrdU-labeled nuclei were clearly observed in cells 48 h after transfer into the inorganic medium, while only weak punctate signals were visible in the chloroplasts. In parallel, the number of FtsZ rings decreased from 6 to only 1. When the cells were transferred from an inorganic medium to a nutrient-enriched medium, the number of cells increased only slightly in the first 12 h after transfer; after this time, however, they started to divide more quickly and increased exponentially. Chloroplast nucleoids changed from punctate to rod-like structures, and active chloroplast DNA synthesis and FtsZ ring formation were observed. On the basis of our results, we conclude that multiple FtsZ ring assembly and chloroplast DNA duplication under nutrient-rich conditions facilitate chloroplast division after transfer to oligotrophic conditions without further duplication of chloroplast DNA and formation of new FtsZ rings.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.