Premium
Identification of proteins of the 40 S ribosomal subunit involved in interaction with initiation factor eIF‐2 in the quaternary initiation complex by means of monospecific antibodies
Author(s) -
Bommer Ulrich-Axel,
Stahl Joachim,
Henske Annemarie,
Lutsch Gudrun,
Bielka Heinz
Publication year - 1988
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(88)81366-8
Subject(s) - protein subunit , eukaryotic large ribosomal subunit , ribosome , ribosomal protein , polyclonal antibodies , ribosomal rna , protein quaternary structure , eukaryotic ribosome , ternary complex , eukaryotic small ribosomal subunit , microbiology and biotechnology , biology , antibody , chemistry , biochemistry , genetics , rna , enzyme , gene
Monospecific polyclonal antibodies against seven proteins of the 40 S subunit of rat liver ribosomes were used to identify ribosomal proteins involved in interaction with initiation factor eIF‐2 in the quaternary initiation complex [eIF‐2 × GMPPCP × [ 3 H]Met‐tRNA f × 40 S ribosomal subunit]. Dimeric immune complexes of 40 S subunits mediated by antibodies against ribosomal proteins S3a, S13/16, S19 and S24 were found to be unable to bind the ternary initiation complex [eIF‐2 × GMPPCP × [ 3 H]Met‐tRNA f ]. In contrast, 40 S dimers mediated by antibodies against proteins S2, S3 and S17 were found to bind the ternary complex. Therefore, from the ribosomal proteins tested, only proteins S3a, S13/16, S19 and S24 are concluded to be involved in eIF‐2 binding to the 40 S subunit.