Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Inhibition of translation initiation complex formation by GE81112 unravels a 16S rRNA structural switch involved in P-site decoding.

Fabbretti, A., Schedlbauer, A., Brandi, L., Kaminishi, T., Giuliodori, A. M., Garofalo, R., et al. (2016). Inhibition of translation initiation complex formation by GE81112 unravels a 16S rRNA structural switch involved in P-site decoding. Proceedings of the National Academy of Sciences of the United States of America, 113(16), E2286-E2295. doi:10.1073/pnas.1521156113.

Item is

Dateien

einblenden: Dateien
ausblenden: Dateien
:
2282884.pdf (Verlagsversion), 3MB
 
Datei-Permalink:
-
Name:
2282884.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Eingeschränkt (UNKNOWN id 303; )
MIME-Typ / Prüfsumme:
application/pdf
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-
:
2282884_Suppl.pdf (Ergänzendes Material), 2MB
Name:
2282884_Suppl.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:
ausblenden:
externe Referenz:
http://www.pnas.org/content/113/16/E2286.full (Verlagsversion)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Fabbretti, A., Autor
Schedlbauer, A., Autor
Brandi, L., Autor
Kaminishi, T., Autor
Giuliodori, A. M., Autor
Garofalo, R.1, Autor           
Ochoa-Lizarralde, B., Autor
Takemoto, C., Autor
Yokoyama, S., Autor
Connell, S. R., Autor
Gualerzi, C. O., Autor
Fucini, P., Autor
Affiliations:
1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              

Inhalt

einblenden:
ausblenden:
Schlagwörter: GE81112; ribosome; X-ray crystallography; protein synthesis; antibiotics
 Zusammenfassung: In prokaryotic systems, the initiation phase of protein synthesis is governed by the presence of initiation factors that guide the transition of the small ribosomal subunit (30S) from an unlocked preinitiation complex (30S preIC) to a locked initiation complex (30SIC) upon the formation of a correct codon-anticodon interaction in the peptidyl (P) site. Biochemical and structural characterization of GE81112, a translational inhibitor specific for the initiation phase, indicates that the main mechanism of action of this antibiotic is to prevent P-site decoding by stabilizing the anticodon stem loop of the initiator tRNA in a distorted conformation. This distortion stalls initiation in the unlocked 30S preIC state characterized by tighter IF3 binding and a reduced association rate for the 50S subunit. At the structural level we observe that in the presence of GE81112 the h44/h45/h24a interface, which is part of the IF3 binding site and forms ribosomal intersubunit bridges, preferentially adopts a disengaged conformation. Accordingly, the findings reveal that the dynamic equilibrium between the disengaged and engaged conformations of the h44/h45/h24a interface regulates the progression of protein synthesis, acting as a molecular switch that senses and couples the 30S P-site decoding step of translation initiation to the transition from an unlocked preIC to a locked 30SIC state.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2016-04-19
 Publikationsstatus: Online veröffentlicht
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.1521156113
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Proceedings of the National Academy of Sciences of the United States of America
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 113 (16) Artikelnummer: - Start- / Endseite: E2286 - E2295 Identifikator: -