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  Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes

Christodoulou, J., Larsson, G., Fucini, P., Connell, S. R., Pertinhez, T. A., Hanson, C. L., et al. (2004). Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes. Proceedings of the National Academy of Sciences, 101(30), 10949-10954. doi:10.1073/pnas.0400928101.

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Genre: Zeitschriftenartikel
Alternativer Titel : Proc Natl Acad Sci U S A

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Christodoulou, John, Autor
Larsson, Göran, Autor
Fucini, Paola1, Autor           
Connell, Sean R.2, Autor           
Pertinhez, Thelma A., Autor
Hanson, Charlotte L., Autor
Redfield, Christina, Autor
Nierhaus, Knud H.1, Autor           
Robinson, Carol V., Autor
Schleucher, Jürgen, Autor
Dobson, Christopher M., Autor
Affiliations:
1Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
2Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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 Zusammenfassung: 15N-1H NMR spectroscopy has been used to probe the dynamic properties of uniformly 15N labeled Escherichia coli ribosomes. Despite the high molecular weight of the complex ({approx}2.3 MDa), [1H-15N] heteronuclear single-quantum correlation spectra contain {approx}100 well resolved resonances, the majority of which arise from two of the four C-terminal domains of the stalk proteins, L7/L12. Heteronuclear pulse-field gradient NMR experiments show that the resonances arise from species with a translational diffusion constant consistent with that of the intact ribosome. Longitudinal relaxation time (T1) and T1{rho} 15N-spin relaxation measurements show that the observable domains tumble anisotropically, with an apparent rotational correlation time significantly longer than that expected for a free L7/L12 domain but much shorter than expected for a protein rigidly incorporated within the ribosomal particle. The relaxation data allow the ribosomally bound C-terminal domains to be oriented relative to the rotational diffusion tensor. Binding of elongation factor G to the ribosome results in the disappearance of the resonances of the L7/L12 domains, indicating a dramatic reduction in their mobility. This result is in agreement with cryoelectron microscopy studies showing that the ribosomal stalk assumes a single rigid orientation upon elongation factor G binding. As well as providing information about the dynamical properties of L7/L12, these results demonstrate the utility of heteronuclear NMR in the study of mobile regions of large biological complexes and form the basis for further NMR studies of functional ribosomal complexes in the context of protein synthesis.

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Sprache(n): eng - English
 Datum: 2004-07-19
 Publikationsstatus: Erschienen
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 Identifikatoren: eDoc: 224266
DOI: 10.1073/pnas.0400928101
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Titel: Proceedings of the National Academy of Sciences
  Alternativer Titel : Proc Natl Acad Sci U S A
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 101 (30) Artikelnummer: - Start- / Endseite: 10949 - 10954 Identifikator: ISSN: 0027-8424