Cross-linking of Met-tRNAfto eIF-2β and to the ribosomal proteins S3a and S6 within the eukaryotic initiation complex, eIF-2-GMPPCP Met-tRNAf-small ribosomal subunit | Zendy

Peter Westermann | Zendy; Odd Nygârd | Zendy; H Bielka | Zendy

Open Access

Cross-linking of Met-tRNA_fto eIF-2β and to the ribosomal proteins S3a and S6 within the eukaryotic initiation complex, eIF-2-GMPPCP Met-tRNA_f-small ribosomal subunit

Author(s) -

Peter Westermann,

Odd Nygârd,

H Bielka

Publication year - 1981

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/9.10.2387

Subject(s) - biology , ribosomal rna , ribosomal protein , ribosome , eukaryotic large ribosomal subunit , transfer rna , protein subunit , eukaryotic small ribosomal subunit , biochemistry , 5.8s ribosomal rna , microbiology and biotechnology , rna , gene

In the quaternary initiation complex, eIF-2.GMPPCP.Met-tRNAf.40S ribosomal subunit, the Met-tRNAf can be cross-linked to the beta subunit of initiation factor eIF-2 as well as to ribosomal proteins S3a and S6 by treatment with the bifunctional reagent, diepoxybutane. Using 40S subunits, modified in advance with the heterobifunctional reagent, methyl-rho-azido-benzoylaminoacetimidate, Met-tRNAf is covalently bound to the same ribosomal proteins (S3a and S6) upon irradiation of the complex with ultraviolet light. Under both conditions proteins S3a and S6, together with a limited number of other ribosomal proteins, are covalently bound to 18S ribosomal RNA.

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