Molecular Architecture of the Neurofilament I. Subunit Arrangement of Neurofilament L Protein in the Intermediatesized Filament英文文献.pdfVIP

J. Mol. Biol. (1990) 211, 857-869 Molecular Architecture of the Neurofilament I. Subunit Arrangement of Neurofilament L Protein in the Intermediate- sized Filament Shin-ii Hisanaga’t, Atsushi Ikai’ and Nobutaka Hirokawa’ ‘Department of Anatomy and Cell Biology, Faculty of Medicine 2Department of Biophysics and Biochemistry, Faculty of Science University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113, Japan (Received 9 May 1989; accepted 30 August 1989) Using the smallest subunit (NF-L) of a neurofilament and a glial fibrillary acidic protein, the subunit arrangement in intermediate filaments was studied by low-angle rotary shadowing. NF-L formed a pair of 70 to 80 nm rods in a low ionic strength solution at pH 6.8. Two 70 to 80 nm rods appeared to associate in an antiparallel manner with an overlap of about 55 nm, almost the same length as the a-helix-rich central rod domain of intermediate filament proteins. The overlap extended for three-beaded segments, present at 22 nm intervals along the pairs of rods. The observations that (1) 70 to 80 nm rods were a predominant structure in a low ionic strength solution at pH 85, (2) the molecular weights of the rod and the pair were measured by sedimentation