Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Structure and dynamics of the mammalian ribosomal pretranslocation complex

Budkevich, T., Giesebrecht, J., Altman, R. B., Munro, J. B., Mielke, T., Nierhaus, K. H., et al. (2011). Structure and dynamics of the mammalian ribosomal pretranslocation complex. Mol Cell, 44(2), 214-24. Retrieved from http://pdn.sciencedirect.com/science?_ob=MiamiImageURL&_cid=272198&_user=28761&_pii=S109727651100757X&_check=y&_origin=article&_zone=toolbar&_coverDate=21-Oct-2011&view=c&originContentFamily=serial&wchp=dGLzVlt-zSkzS&md5=7955fd02fcf620b68260bfdefd7032ae/1-s2.0-S109727651100757X-main.pdf.

Item is

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Budkevich, T.1, Autor           
Giesebrecht, J., Autor
Altman, R. B., Autor
Munro, J. B., Autor
Mielke, T.2, Autor           
Nierhaus, K. H.3, Autor           
Blanchard, S. C., Autor
Spahn, C. M.4, Autor           
Affiliations:
1Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433549              
2Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
4Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

Inhalt

einblenden:
ausblenden:
Schlagwörter: Animals; Anti-Bacterial Agents/chemistry; Binding Sites; Cryoelectron Microscopy; Cycloheximide/chemistry; Fluorescence Resonance Energy Transfer; Models, Molecular; Nucleic Acid Conformation; RNA, Transfer, Amino Acyl/ chemistry/metabolism; Rabbits; Ribosomes/ chemistry/metabolism
 Zusammenfassung: Although the structural core of the ribosome is conserved in all kingdoms of life, eukaryotic ribosomes are significantly larger and more complex than their bacterial counterparts. The extent to which these differences influence the molecular mechanism of translation remains elusive. Multiparticle cryo-electron microscopy and single-molecule FRET investigations of the mammalian pretranslocation complex reveal spontaneous, large-scale conformational changes, including an intersubunit rotation of the ribosomal subunits. Through structurally related processes, tRNA substrates oscillate between classical and at least two distinct hybrid configurations facilitated by localized changes in their L-shaped fold. Hybrid states are favored within the mammalian complex. However, classical tRNA positions can be restored by tRNA binding to the E site or by the eukaryotic-specific antibiotic and translocation inhibitor cycloheximide. These findings reveal critical distinctions in the structural and energetic features of bacterial and mammalian ribosomes, providing a mechanistic basis for divergent translation regulation strategies and species-specific antibiotic action.

Details

einblenden:
ausblenden:
Sprache(n):
 Datum: 2011
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Mol Cell
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 44 (2) Artikelnummer: - Start- / Endseite: 214 - 24 Identifikator: ISSN: 1097-4164 (Electronic) 1097-2765 (Linking)