Literature DB >> 361396

Polynucleotide-protein interactions in the translation system. Detection of contacts between some ribosomal split proteins and 16-S RNA in 30-S subunits of Escherichia coli ribosomes.

M F Turchinsky, N E Broude, K S Kussova, G G Abduraschidova, E V Muchamedganova, I N Schatsky, T F Bystrova, E I Budowsky.   

Abstract

Direct contacts between 16-S RNA and split proteins S2, S3, S5, S14 and S21 inside the 30-S subunit of Escherichia coli ribosomes were evidenced by the formation of ultraviolet-induced (lambda = 254 nm) RNA-protein cross-links. 30-S subunits were reassembled from core particles and a mixture of split proteins containing in each case a single 125I-labelled protein. All the proteins tested are cross-linked as a result of a single-hit process; proteins S3 and S21 were cross-linked at the highest rate.

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Year:  1978        PMID: 361396     DOI: 10.1111/j.1432-1033.1978.tb12577.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

Review 1.  Contact-site cross-linking agents.

Authors:  G R Kunkel; M Mehrabian; H G Martinson
Journal:  Mol Cell Biochem       Date:  1981-01-20       Impact factor: 3.396

2.  Polynucleotide-protein interactions in the translation system. Identification of proteins interacting with tRNA in the A- and P-sites of E. coli ribosomes.

Authors:  G G Abdurashidova; M F Turchinsky; K A Aslanov; E I Budowsky
Journal:  Nucleic Acids Res       Date:  1979-08-24       Impact factor: 16.971

  2 in total

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