Literature DB >> 6278435

Study on conformational states of Escherichia coli tRNAPhe in solution by a modulation-free ESR-spectrometer.

G N Bondarev, V V Isaev-Ivanov, L S Isaeva-Ivanova, S V Kirillov, A R Kleiner, A F Lepekhin, V B Odinzov, V N Fomichev.   

Abstract

A modulation free Electron Spin Resonance spectrometer was used for the registration of spectral absorption lines of a spin-labeled Escherichia coli phenylalanine tRNA in solution with low (less than 0.1%) line shape distortion. The analysis of line shape of two different spin-labels introduced into position 8 revealed that phenylalanine tRNA in solution exists as a mixture of two conformers, the equilibria between conformers being dependent on pH, concentration of magnesium and functional state of tRNA (deacylated, aminoacylated or peptidylated). There are no overall structural rearrangements upon aminoacylation or peptidylation of tRNA. The observed small changes of spectral line shape can be assigned to shifts in conformational equilibria.

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Year:  1982        PMID: 6278435      PMCID: PMC326226          DOI: 10.1093/nar/10.3.1113

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  13 in total

1.  A speculation on the origin of protein synthesis.

Authors:  F H Crick; S Brenner; A Klug; G Pieczenik
Journal:  Orig Life       Date:  1976-12

2.  Aminoacyl-tRNA binding at the recognition site is the first step of the elongation cycle of protein synthesis.

Authors:  J A Lake
Journal:  Proc Natl Acad Sci U S A       Date:  1977-05       Impact factor: 11.205

3.  On the structure and conformational dynamics of yeast phenylalanine-accepting transfer ribonucleic acid in solution.

Authors:  M Ehrenberg; R Rigler; W Wintermeyer
Journal:  Biochemistry       Date:  1979-10-16       Impact factor: 3.162

4.  The mechanism of codon-anticodon interaction in ribosomes. Heterogeneity of tRNA complexes with 70-S ribosomes of Escherichia coli.

Authors:  S V Kirillov; V I Makhno; V B Odinzov; Y P Semenkov
Journal:  Eur J Biochem       Date:  1978-08-15

5.  Improvement of the spin-labelling technique by the use of a radioactive spin label.

Authors:  N C Price
Journal:  FEBS Lett       Date:  1973-11-01       Impact factor: 4.124

6.  Proton magnetic resonance studies on the conformation of the hexanucleotide, GmpApApYpApsiP, and Related fragments from the anticodong loop of baker's yeast phenylalanine transfer ribonucleic acid.

Authors:  L S Kan; P O Ts'o; F von der Haar; M Sprinzl; F Cramer
Journal:  Biochemistry       Date:  1975-07-15       Impact factor: 3.162

7.  1H nuclear magnetic resonance of modified bases of valine transfer ribonucleic acid (Escherichia coli). A direct monitor of sequential thermal unfolding.

Authors:  R V Kastrup; P G Schmidt
Journal:  Biochemistry       Date:  1975-08-12       Impact factor: 3.162

8.  Evidence for a conformational change in tRNAPhe upon aminoacylation.

Authors:  M Caron; N Brisson; H Dugas
Journal:  J Biol Chem       Date:  1976-03-10       Impact factor: 5.157

9.  A spin label study of the thermal unfolding of secondary and tertiary structure in E. colic transfer RNAs.

Authors:  M Caron; H Dugas
Journal:  Nucleic Acids Res       Date:  1976-01       Impact factor: 16.971

10.  The interconversion of conformers of phenylalanyl-tRNA with different affinity to 70S ribosomes of Escherichia coli.

Authors:  S V Kirillov; V B Odinzov
Journal:  Nucleic Acids Res       Date:  1978-05       Impact factor: 16.971

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  2 in total

Review 1.  Site-directed spin labeling studies on nucleic acid structure and dynamics.

Authors:  Glenna Z Sowa; Peter Z Qin
Journal:  Prog Nucleic Acid Res Mol Biol       Date:  2008

2.  Paving the Road Toward Exploiting the Therapeutic Effects of Ginsenosides: An Emphasis on Autophagy and Endoplasmic Reticulum Stress.

Authors:  Milad Ashrafizadeh; Shima Tavakol; Reza Mohammadinejad; Zahra Ahmadi; Habib Yaribeygi; Tannaz Jamialahmadi; Thomas P Johnston; Amirhossein Sahebkar
Journal:  Adv Exp Med Biol       Date:  2021       Impact factor: 2.622

  2 in total

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