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Differences in 23 S rRNA‐protein neighbourhood in Escherichia coli 70 S ribosomes and 70 S initiation complex
Author(s) -
Chistyakov P.G.,
Venjaminova A.G,
Vladimirov S.N.,
Graifer D.M.,
Kasakov S.A.,
Karpova C.G
Publication year - 1989
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(89)80282-0
Subject(s) - ribosome , ribosomal rna , ribosomal protein , eukaryotic ribosome , escherichia coli , chemistry , transfer rna , biochemistry , protein biosynthesis , biology , microbiology and biotechnology , rna , gene
rRNA‐protein cross‐links in free E. Coli 35 S‐labeled 70 S ribosomes and in the initiation complex 35 ‐labeled 70 S ribosome · AUGU 6 · Met f ‐tRNA Met f were studied with the aid of a new type of binuclear (PtII) compound — dichlorotetra‐ammine (1,6‐hexamethylenediaminediplatinum) dichloride. The use of this reagent allowed us to reveal differences in the rRNA‐protein neighbourhood in free 70 S ribosomes and in the initiation complex. Proteins L3, L6, L23 and L25 were shown to cross‐link to 23 S rRNA only in the initiation complex, whereas proteins L1, L13, L14, L16. L17, L18, L22, L28 and S1 did so in both free ribosomes and the complex. 16 S rRNA was found to be cross‐linked preferentially to a single protein, S1, in both states of the ribosomes.