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Studies on interaction of 5 S RNA with ribosomal proteins
Author(s) -
Kärgel H.-J.,
Stahl J.,
Gross B.,
Knespel S.,
Bielka H.,
Saarma M.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80889-x
Subject(s) - ribosomal protein , ribosomal rna , rna , microbiology and biotechnology , protein subunit , blot , polyacrylamide gel electrophoresis , nitrocellulose , eukaryotic large ribosomal subunit , gel electrophoresis , biochemistry , chemistry , biology , ribosome , enzyme , gene , membrane
Proteins of the large ribosomal subunit of rat liver (TP 60) were immobilized by diffusion transfer onto nitrocellulose after two‐dimensional polyacrylamide gel electrophoresis (2‐D PAGE). Incubation of the TP 60 blots with 32 P‐labeled 5 S RNA under defined ionic conditions (300 mM KCl, 20 mM MgCl 2 ) resulted in specific binding to a limited set of ribosomal proteins consisting of proteins L3, L4, L6, L13/15 and — to a lesser extent — L7 and L19. Under identical conditions, blots with proteins of the small ribosomal subunit (TP 40) did not bind 5 S RNA.