Are the terminal domains in intermediate filaments organized as octameric complexes? Reevaluation of a recent suggestion.
Recently L. M. Milam and H. Erickson ((1985) J. Ultrastruc. Res. 90, 251-260) reported the isolation of a particle thought to be an octomeric complex of the terminal domains of desmin. This complex was isolated after trypsin treatment of intact filaments. As the existence of such a complex would place important restrictions on the possible packing modes of subunits within the filament we have repeated their procedure and additionally characterized the particle in question by detailed protein chemical data. We find that the particle is not derived from the terminal domains but instead comprises a portion of the carboxy-terminal half of the alpha-helical rod domain. We further show that the terminal domains are very rapidly digested into small peptides during the trypsin treatment of the filaments. No inferences on the structure of intermediate filament are therefore possible from the data in the original report.
D000818:Animals; D002645:Chickens; D002850:Chromatography, Gel; D003599:Cytoskeleton / Q000032:analysis*; D003893:Desmin / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007382:Intermediate Filaments / Q000032:analysis*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin
D003893:Desmin; D010446:Peptide Fragments; D014357:Trypsin