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RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi, Molekylärbiologi. (Sanyal)
Vise andre og tillknytning
2007 (engelsk)Inngår i: Cell, ISSN 0092-8674, E-ISSN 1097-4172, Vol. 129, nr 5, s. 929-941Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

During translation termination, class II release factor RF3 binds to the ribosome to promote rapid dissociation of a class I release factor (RF) in a GTP-dependent manner. We present the crystal structure of E. coli RF3•GDP, which has a three-domain architecture strikingly similar to the structure of EF-Tu•GTP. Biochemical data on RF3 mutants show that a surface region involving domains II and III is important for distinct steps in the action cycle of RF3. Furthermore, we present a cryo-electron microscopy (cryo-EM) structure of the posttermination ribosome bound with RF3 in the GTP form. Our data show that RF3•GTP binding induces large conformational changes in the ribosome, which break the interactions of the class I RF with both the decoding center and the GTPase-associated center of the ribosome, apparently leading to the release of the class I RF.

sted, utgiver, år, opplag, sider
2007. Vol. 129, nr 5, s. 929-941
Emneord [en]
CHEMBIO, PROTEINS
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-12924DOI: 10.1016/j.cell.2007.03.050ISI: 000247084600013PubMedID: 17540173OAI: oai:DiVA.org:uu-12924DiVA, id: diva2:40694
Tilgjengelig fra: 2008-06-10 Laget: 2008-06-10 Sist oppdatert: 2017-12-11bibliografisk kontrollert

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