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Laser Raman studies of the 5 S rRNA‐protein L5 complex of rat liver ribosomes
Author(s) -
Fabian Heinz,
Böhm Siegfried,
Carius Wolfgang,
Misselwitz Rolf,
Welfle Heinz
Publication year - 1983
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(82)80622-4
Subject(s) - ribosome , ribosomal rna , ribosomal protein , raman spectroscopy , uracil , guanine , cytosine , biochemistry , chemistry , biology , microbiology and biotechnology , dna , rna , nucleotide , physics , optics , gene
The effects of ribosomal protein L5 on the conformation of 5 S rRNA in the 5 S rRNA—protein L5 complex extracted from rat liver ribosomes have been studied by laser Raman spectroscopy. A comparison of the spectra shows small protein‐induced conformational changes in the 5 S rRNA, but most of the base‐paired regions appear to be present in the complex with protein L5 as well as in the free 5 S rRNA. Furthermore specific interactions between 5 S rRNA and protein L5 are indicated. Cytosine (and/or uracil) residues in single‐stranded regions and the N(7) of guanine are engaged in interactions with the protein as suggested by the Raman data.