Cytokinesis by a contractile ring in the primitive red alga Cyanidium caldarium RK-1.

To better understand the mechanism of cytokinesis in eukaryotes, the behavior of the contractile ring in the two unicellular primitive red algae Cyanidioschyzon merolae and Cyanidium caldarium RK-1, which have the smallest genome size among eukaryotes, was examined by fluorescein isothiocyanate (FITC)-phalloidin fluorescence microscopy, fluorometry using a video-intensified microscope photoncounting system, transmission electron microscopy and immunoblotting techniques. Cells in each alga contained one nucleus, one mitochondrion and one chloroplast, which were aligned in that order. During cytokinesis in C. merolae, a contractile ring was not observed by fluorescence microscopy or by transmission electron microscopy. In contrast, in C. caldarium RK-1, a contractile ring appeared at the equatorial region of the dividing cells and began to contract from the side of the chloroplast. During contraction of this ring, the total fluorescent intensities due to FITC-phalloidin remained constant. Electron microscopy revealed outer and inner bands approximately 80 nm wide and 9 nm thick which ran parallel to each other just beneath the cell membrane. These bands were visible at the equator of the cell just before the initiation of cytokinesis and constricted from the pole of the chloroplast. Both bands increased in width as cleavage progressed. The inner ring consisted of a bundle of approximately 20 actin-like filaments which were arranged as a raft. In the outer ring, such fine filaments were not visible. It seems likely that the bundle of filaments, known as the contractile ring, is composed of two different elements: an inner band of actin filaments and an outer band of unknown materials.(ABSTRACT TRUNCATED AT 250 WORDS)