Rotational Relaxation of 70S Ribosomes by a Depolarization Method Using Triplet Probes

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1977 Apr 1

PMID 323851

Citations 11

Authors

D Lavalette

B Amand

F POCHON

Affiliations

Soon will be listed here.

Abstract

Rotational relaxation on the microsecond time scale has been followed by a depolarization technique using the properties of the long-lived triplet state of covalently bound labels. Two triplet probes, which efficiently bind to ribosomal proteins, are described. The rotational correlation time of 70S ribosomes of Escherichia coli has been measured. The average hydrodynamic radius of the functionally active 70S particle in solution has been estimated to 147 A. A concentration dependence of the correlation time has been observed, which may result from an association of the 70S ribosomes to form 100S dimers.

Citing Articles

The ribosome lowers the entropic penalty of protein folding.

Streit J, Bukvin I, Chan S, Bashir S, Woodburn L, Wlodarski T Nature. 2024; 633(8028):232-239.

PMID: 39112704 PMC: 11374706. DOI: 10.1038/s41586-024-07784-4.

Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy.

Burridge C, Waudby C, Wlodarski T, Cassaignau A, Cabrita L, Christodoulou J Chem Sci. 2021; 12(39):13120-13126.

PMID: 34745542 PMC: 8513902. DOI: 10.1039/d1sc04313g.

Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.

Cassaignau A, Wlodarski T, Chan S, Woodburn L, Bukvin I, Streit J Nat Chem. 2021; 13(12):1214-1220.

PMID: 34650236 PMC: 8627912. DOI: 10.1038/s41557-021-00796-x.

Optimal design of adaptively sampled NMR experiments for measurement of methyl group dynamics with application to a ribosome-nascent chain complex.

Waudby C, Burridge C, Christodoulou J J Magn Reson. 2021; 326:106937.

PMID: 33706222 PMC: 7613274. DOI: 10.1016/j.jmr.2021.106937.

Size, stoichiometry, and organization of soluble LC3-associated complexes.

Kraft L, Nguyen T, Vogel S, Kenworthy A Autophagy. 2014; 10(5):861-77.

PMID: 24646892 PMC: 4768459. DOI: 10.4161/auto.28175.

References

Rinderknecht H . Ultra-rapid fluorescent labelling of proteins. Nature. 1962; 193:167-8. DOI: 10.1038/193167b0. View

COHEN S, Lichtenstein J . Polyamines and ribosome structure. J Biol Chem. 1960; 235:2112-6. View

Weber G . Polarization of the fluorescence of macromolecules. I. Theory and experimental method. Biochem J. 1952; 51(2):145-55. PMC: 1197814. DOI: 10.1042/bj0510145. View

Favaudon V, POCHON F . Magnesium dependence of the association kinetics of Escherichia coli ribosomal subunits. Biochemistry. 1976; 15(18):3903-12. DOI: 10.1021/bi00663a001. View

WELTMAN J, Szaro R, Frackelton Jr A, Dowben R, Bunting J, Cathou B . N-(3-pyrene)maleimide: a long lifetime fluorescent sulfhydryl reagent. J Biol Chem. 1973; 248(9):3173-7. View

Cone R . Rotational diffusion of rhodopsin in the visual receptor membrane. Nat New Biol. 1972; 236(63):39-43. DOI: 10.1038/newbio236039a0. View

Naqvi K, Gonzalez-Rodriguez J, Cherry R, Chapman D . Spectroscopic technique for studying protein rotation in membranes. Nat New Biol. 1973; 245(147):249-51. DOI: 10.1038/newbio245249a0. View

Cherry R, Schneider G . A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 2: Determination of rotational correlation times of proteins in solution. Biochemistry. 1976; 15(17):3657-61. DOI: 10.1021/bi00662a002. View

Koppel D . Study of Escherichia coli ribosomes by intensity fluctuation spectroscopy of scattered laser light. Biochemistry. 1974; 13(13):2712-9. DOI: 10.1021/bi00710a009. View

10.

Wu C, Yarbrough L . N-(1-pyrene)maleimide: a fluorescent cross-linking reagent. Biochemistry. 1976; 15(13):2863-8. DOI: 10.1021/bi00658a025. View

11.

Huang K, Cantor C . Surface topography of the 30 s Escherichia coli ribosomal subunit: reactivity towards fluorescein isothiocyanate. J Mol Biol. 1972; 67(2):265-75. DOI: 10.1016/0022-2836(72)90240-9. View

12.

Junge W, Eckhof A . On the orientation of chlorophyll-a1 in the functional membrane of photosynthesis. FEBS Lett. 1973; 36(2):207-12. DOI: 10.1016/0014-5793(73)80370-9. View

13.

Moore P . Reaction of N-ethyl maleimide with the ribosomes of Escherichia coli. J Mol Biol. 1971; 60(1):169-84. DOI: 10.1016/0022-2836(71)90456-6. View

14.

Eikenberry E, Bickle T, Traut R, Price C . Separation of large quantities of ribosomal subunits by zonal ultracentrifugation. Eur J Biochem. 1970; 12(1):113-6. DOI: 10.1111/j.1432-1033.1970.tb00827.x. View

15.

Kaltschmidt E, WITTMANN H . Ribosomal proteins. VII. Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Anal Biochem. 1970; 36(2):401-12. DOI: 10.1016/0003-2697(70)90376-3. View

16.

Hill W, Thompson J, Anderegg J . X-ray scattering study of ribosomes from Escherichia coli. J Mol Biol. 1969; 44(1):89-102. DOI: 10.1016/0022-2836(69)90406-9. View

17.

Kurland C . The requirements for specific sRNA binding by ribosomes. J Mol Biol. 1966; 18(1):90-108. DOI: 10.1016/s0022-2836(66)80079-7. View

18.

Schechter N, Elson D, SPITNIK-ELSON P . Structural alterations in the 30 S ribosomal subunit of Escherichia coli observed with the fluorescent probe N-(3-pyrene) maleimide. FEBS Lett. 1975; 57(2):149-52. DOI: 10.1016/0014-5793(75)80704-6. View

19.

Ginzburg I, Zamir A . Functional roles and interactions of sulfhydryl proteins of 30 S ribosomal subunits. J Mol Biol. 1976; 100(3):387-98. DOI: 10.1016/s0022-2836(76)80070-8. View

20.

Ginzburg I, Zamir A . Characterization of different conformational forms of 30 S ribosomal subunits in isolated and associated states: possible correlations between structure and function. J Mol Biol. 1975; 93(4):465-76. DOI: 10.1016/0022-2836(75)90240-5. View