Protein topography of the 40 S ribosomal subunit from Saccharomyces cerevisiae as shown by chemical cross-linking

摘要: Abstract Protein-protein cross-linking was used to examine the spatial arrangement of proteins within 40 S ribosomal subunits Saccharomyces cerevisiae. Purified were treated with either 2-iminothiolane or dimethyl 3,3'-dithiobispropionimidate under conditions such that particle intact and formation subunit dimers minimized. Proteins extracted from fractionated on Sephadex G-150 by acid-urea-polyacrylamide gel electrophoresis. Cross-linked in these fractions analyzed two-dimensional diagonal sodium dodecyl sulfate-polyacrylamide Constituent members cross-linked pairs radiolabeled 125I identified electrophoresis comparison nonradioactive protein markers. Forty-two involving 25 32 identified. Many detected several dimers. These multiple cross-links form foci for construction a schematic model subunit.