Open AccessThe Importance of Escherichia coli Ribosomal Proteins L1, L11 and L16 for the Association of Ribosomal Subunits and the Formation of the 70‐S Initiation Complex
Author(s) -
KAZEMIE Mirabotalib
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02398.x
Subject(s) - protein subunit , sephadex , ribosomal rna , ribosomal protein , chemistry , escherichia coli , yeast , biochemistry , chromatography , ribosome , enzyme , rna , gene
50‐S subunits were washed with LiCl solutions of different concentrations. After washing with 1 M LiCl solution the particles lost their ability to attach either to 30‐S subunits or to the AUG · 30‐S subunit · fMet‐tRNA fMet complex or to a poly(U) · 30‐S subunit · Phe‐tRNA Phe complex. Those proteins which were removed by LiCl were fractionated on a Sephadex G‐100 column. Of the fractionated proteins only the combinations L1 and L11 or L1 and L16 were essential for the association of 50‐S 1.0 cores (particles prepared by washing 50‐S subunits in 1.0 M LiCl) with 30‐S subunits. These three proteins were also required for the formation of a stable complex between 50‐S 1.0 cores, mRNA, 30‐S subunits and aminoacyl‐tRNA.