Crystal structure of the ribosome recycling factor bound to the ribosome

Albert Weixlbaumer; Sabine Petry; Christine M. Dunham; Maria Selmer; Ann C. Kelley; V. Ramakrishnan

doi:10.1038/nsmb1282

Crystal structure of the ribosome recycling factor bound to the ribosome

Albert Weixlbaumer, Sabine Petry, Christine M. Dunham, Maria Selmer, Ann C. Kelley, V. Ramakrishnan

Research output: Contribution to journal › Article › peer-review

90 Scopus citations

Abstract

In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNA^fMet in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.

Original language	English (US)
Pages (from-to)	733-737
Number of pages	5
Journal	Nature Structural and Molecular Biology
Volume	14
Issue number	8
DOIs	https://doi.org/10.1038/nsmb1282
State	Published - Aug 2007
Externally published	Yes

All Science Journal Classification (ASJC) codes

Molecular Biology
Structural Biology

Access to Document

10.1038/nsmb1282

Cite this

@article{98390ddf7c1a4c7c87e9b2f44fa9999a,

title = "Crystal structure of the ribosome recycling factor bound to the ribosome",

abstract = "In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNAfMet in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.",

author = "Albert Weixlbaumer and Sabine Petry and Dunham, {Christine M.} and Maria Selmer and Kelley, {Ann C.} and V. Ramakrishnan",

note = "Funding Information: We thank F. Murphy for help with data collection during optimization of crystallization conditions, M. MacDonald for help with screening at beamline 14.1 at the Synchrotron Radiation Source, and R. Ravelli, J. McCarthy and G. Leonard at beamlines ID14-1, ID14-3 and ID14-4 at the ESRF for help with screening and data collection. This work was supported by the Medical Research Council (UK), the US National Institutes of Health and the Agouron Institute, and fellowships from the Austrian Academy of Sciences (A.W.), the Boehringer Ingelheim Fonds (S.P.), the American Cancer Society (C.M.D.) and the Wenner-Gren foundation (M.S.).",

year = "2007",

month = aug,

doi = "10.1038/nsmb1282",

language = "English (US)",

volume = "14",

pages = "733--737",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Publishing Group",

number = "8",

}

TY - JOUR

T1 - Crystal structure of the ribosome recycling factor bound to the ribosome

AU - Weixlbaumer, Albert

AU - Petry, Sabine

AU - Dunham, Christine M.

AU - Selmer, Maria

AU - Kelley, Ann C.

AU - Ramakrishnan, V.

N1 - Funding Information: We thank F. Murphy for help with data collection during optimization of crystallization conditions, M. MacDonald for help with screening at beamline 14.1 at the Synchrotron Radiation Source, and R. Ravelli, J. McCarthy and G. Leonard at beamlines ID14-1, ID14-3 and ID14-4 at the ESRF for help with screening and data collection. This work was supported by the Medical Research Council (UK), the US National Institutes of Health and the Agouron Institute, and fellowships from the Austrian Academy of Sciences (A.W.), the Boehringer Ingelheim Fonds (S.P.), the American Cancer Society (C.M.D.) and the Wenner-Gren foundation (M.S.).

PY - 2007/8

Y1 - 2007/8

N2 - In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNAfMet in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.

AB - In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNAfMet in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.

UR - http://www.scopus.com/inward/record.url?scp=34547664728&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34547664728&partnerID=8YFLogxK

U2 - 10.1038/nsmb1282

DO - 10.1038/nsmb1282

M3 - Article

C2 - 17660830

AN - SCOPUS:34547664728

SN - 1545-9993

VL - 14

SP - 733

EP - 737

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 8

ER -

Crystal structure of the ribosome recycling factor bound to the ribosome

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this