Cyclic production of tension force in the plasmodial strand of Physarum polycephalum and its relation to microfilament morphology.
Cyclic contraction and relaxation of plasmodial strands of Physarum polycephalum were measured under both isotonic and isometric conditions, and their relation to changes in microfilament (MF) morphology was investigated. The contraction-relaxation rhythm of a strand segment was insignificant and irregular immediately after isolation from the mother plasmodium. It became regular half an hour later when local minute rhythms were synchronized spontaneously. If a strand kept under isotonic conditions was loaded with a heavier weight or a strand kept under isometric conditions was stretched a few times, the amplitude of each contraction wave was enhanced. After a strand had been thus conditioned, it was fixed at a selected phase of the contraction-relaxation cycle under both isotonic and isometric conditions. The state of MFs changed strikingly according to the phase of the contraction cycle. In the shortening phase of the strand under isotonic contractions, MFs with a diameter of 6--7 nm were arranged parallel to each other to form large compact bundles in which adjacent filaments were bridged with cross linkages. Among these MFs, thicker filaments were sporadically scattered. At about the phase of minimal strand length, most of the MFs became kinky and formed networks. In the elongating phase, new loose bundles of MFs developed from the network. These loose bundles became compact again when the strand reached its maximal elongation phase. In the isometric contraction, MFs in the increasing tension phase were nearly the same as those in the shortening phase in isotonic contraction. Around the maximal tension phase, dense areas of MFs appeared along the bundles in place of the network formed in the isotonic contraction phase. These areas were closely packed, with MFs arranged parallel to each other. In the decreasing and minimal tension phases in isometric contraction, MFs were arranged similarly to those in the elongating and maximally elongated phases, respectively, in isotonic contraction. Alternation between the straight bundle and fine network configuration of the MFs observed in isotonic contraction was inconspicuous in isometric contraction. This was probably due to spatial restriction of shortening under isometric contraction. The results are interpreted in terms of cyclic changes of the aggregation pattern of the MFs in the form of F-actin, as opposed to the possibility that the contraction-relaxation cycles depend on cyclic G-F transformation of actin.
D001696:Biomechanical Phenomena; D003285:Contractile Proteins / Q000502:physiology; D003593:Cytoplasm / Q000502:physiology*; D003599:Cytoskeleton / Q000502:physiology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D010507:Periodicity; D010804:Physarum / Q000502:physiology* / Q000648:ultrastructure
D003285:Contractile Proteins