Literature DB >> 3512304

Are there proteins between the ribosomal subunits? Hot tritium bombardment experiments.

M M Yusupov, A S Spirin.   

Abstract

The hot tritium bombardment technique [(1976) Dokl. Akad. Nauk SSSR 228, 1237-1238] was used for studying the surface localization of ribosomal proteins on Escherichia coli ribosomes. The degree of tritium labeling of proteins was considered as a measure of their exposure (surface localization). Proteins S1, S4, S7, S9 and/or S11, S12 and/or L20, S13, S18, S20, S21, L5, L6, L7/L12, L10, L11, L16, L17, L24, L26 and L27 were shown to be the most exposed on the ribosome surface. The sets of exposed ribosomal proteins on the surface of 70 S ribosomes, on the one hand, and the surfaces of 50 S and 30 S ribosomal subunits in the dissociated state, on the other, were compared. It was found that the dissociation of ribosomes into subunits did not result in exposure of additional ribosomal proteins. The conclusion was drawn that proteins are absent from the contacting surfaces of the ribosomal subunits.

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Year:  1986        PMID: 3512304     DOI: 10.1016/0014-5793(86)80332-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Modelling protein three-dimensional structure using tritium planigraphy.

Authors:  A Gedrovich; A Shishkov; V Goldanskii; L Baratova; N Grebenshchikov; A Efimov
Journal:  Eur Biophys J       Date:  1991       Impact factor: 1.733

2.  Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique.

Authors:  D E Agafonov; V A Kolb; A S Spirin
Journal:  Proc Natl Acad Sci U S A       Date:  1997-11-25       Impact factor: 11.205

3.  A protein residing at the subunit interface of the bacterial ribosome.

Authors:  D E Agafonov; V A Kolb; I V Nazimov; A S Spirin
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

4.  Flavin-dependent alcohol oxidase from the yeast Pichia pinus. Spatial localization of the coenzyme FAD in the protein structure: hot-tritium bombardment and ESR experiments.

Authors:  A Z Averbakh; N D Pekel; V I Seredenko; A V Kulikov; R I Gvozdev; I P Rudakova
Journal:  Biochem J       Date:  1995-09-01       Impact factor: 3.857

  4 in total

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