Occurrence of proteinaceous 10-nm filaments throughout the cytoplasm of algae of the order Dasycladales.
Previously, whole-mount electron microscopy of nuclei extruded together with residual cytoplasm from the rhizoids of several algal species of the order Dasycladales has revealed the occurrence of an intra- and perinuclear network of 10-nm filaments morphologically indistinguishable from that of mammalian vimentin intermediate filaments. The present investigation demonstrates the existence of a filament system throughout the cytoplasm of the rhizoid, stalk, and apical tip of these giant cells. However, while the perinuclear 10-nm filaments interconnecting the nuclear surface with a perinuclear layer of large, electron-dense bodies filled with nucleoprotein material are of smooth appearance, those continuing within and beyond the perinuclear bodies are densely covered with differently sized, globular structures and, therefore, are of a very rough appearance. The filaments in the very apical tip of the cells are mainly of the smooth type. The transition from smooth to rough filaments seems to occur in the numerous perinuclear dense bodies surrounding the large nucleus. Digestion of the rough filaments with proteinase K removes the globules from the filament surface, revealing that throughout the nonvacuolar, intracellular space the filaments have the same basic 10-nm structure. On the other hand, gold-conjugated RNase A strongly binds to the filament-attached globules but not to the smooth, perinuclear, and the proteinase K-treated, rough filaments. In addition, an antibody raised against Xp54, a highly conserved protein which in Xenopus oocytes is an integral component of stored mRNP particles, decorates the rough but not the smooth 10-nm filaments. These results support the notion that the 10-nm filament system of Dasycladales cells plays a role in the transient storage of ribonucleoprotein particles in the cytoplasm and possibly fulfils a supportive function in the actomyosin-based transport of such material to various cytological destinations.
Berger
S
S
Max-Planck-Institut für Zellbiologie, Ladenburg, Germany.
Wittke
W
W
Traub
P
P
D000460:Chlorophyta / Q000378:metabolism* / Q000648:ultrastructure*; D003593:Cytoplasm / Q000378:metabolism / Q000648:ultrastructure; D019286:Endopeptidase K / Q000378:metabolism; D007382:Intermediate Filaments / Q000378:metabolism* / Q000648:ultrastructure*; D034882:Lamins; D009687:Nuclear Proteins / Q000378:metabolism; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000378:metabolism; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D034882:Lamins; D009687:Nuclear Proteins; D012316:RNA Nucleotidyltransferases; D012259:Ribonuclease, Pancreatic; D014357:Trypsin; D019286:Endopeptidase K; D020365:RNA Helicases