A comparison of accessibility of ribosomal proteins on free and membrane-bound ribosomes: the ribosomal proteins potentially involved in ribosome-membrane binding.
The relative accessibility of rat liver ribosomal proteins to reductive methylation was examined using membrane-bound and free ribosomes. Comparisons indicated that 12-13 large ribosomal proteins are masked by ribosomal association with membranes. These consisted of L8, L10, L17, L26-28, L31 and L36, and probably also include L4, L5, L7 and L29. These proteins seem to surround a region centered about L3 and may partly define a ribosomal channel through which the nascent peptide emerges. Approx. 10-20% of the large ribosomal subunit surface area is shielded by the membrane.
Kisilevsky
R
R
Department of Pathology, Queen's University, Kingston, Canada.
Gore
J
J
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005260:Female; D008745:Methylation; D051381:Rats; D011919:Rats, Inbred Strains; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure
D012269:Ribosomal Proteins