Crystal structure analysis of the translation factor RF3 (release factor 3)

Kiyohito Kihira; Yoshihiro Shimizu; Yasuhito Shomura; Naoki Shibata; Masaya Kitamura; Atsushi Nakagawa; Takuya Ueda; Kozo Ochi; Yoshiki Higuchi

doi:10.1016/j.febslet.2012.08.029

Crystal structure analysis of the translation factor RF3 (release factor 3)

Kiyohito Kihira, Yoshihiro Shimizu, Yasuhito Shomura, Naoki Shibata, Masaya Kitamura, Atsushi Nakagawa, Takuya Ueda, Kozo Ochi, Yoshiki Higuchi^*

^*Corresponding author for this work

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

24 Citations (Scopus)

Abstract

The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3′,5′-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0 Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.

Original language	English
Pages (from-to)	3705-3709
Number of pages	5
Journal	FEBS Letters
Volume	586
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2012.08.029
Publication status	Published - 2012 Oct 19
Externally published	Yes

Keywords

GTPase
Release factor
Ribosome
Stringent response
Translation

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2012.08.029

Cite this

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title = "Crystal structure analysis of the translation factor RF3 (release factor 3)",

abstract = "The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3′,5′-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0 {\AA}, respectively. ppGpp is involved in the so-called {"}stringent response{"} of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.",

keywords = "GTPase, Release factor, Ribosome, Stringent response, Translation",

author = "Kiyohito Kihira and Yoshihiro Shimizu and Yasuhito Shomura and Naoki Shibata and Masaya Kitamura and Atsushi Nakagawa and Takuya Ueda and Kozo Ochi and Yoshiki Higuchi",

note = "Funding Information: We are grateful to Dr. N. Shimizu, Dr. M. Kawamoto and Dr. M. Yamamoto at SPring-8 for their help during data collection at synchrotron beamline BL41XU. This work was supported in part by Grants-in-Aid from the GCOE Programs (YH) and for Scientific Research from MEXT ( 18GS0207 ) (YH), 22370061 (YH), and 22657031 (YH), the Japanese Aerospace Exploration Agency Project (YH). We also thank the NBRP (NIG, Japan): E. coli for providing the ASKA clone (−) JW5873 used in this work. ",

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doi = "10.1016/j.febslet.2012.08.029",

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T1 - Crystal structure analysis of the translation factor RF3 (release factor 3)

AU - Kihira, Kiyohito

AU - Shimizu, Yoshihiro

AU - Shomura, Yasuhito

AU - Shibata, Naoki

AU - Kitamura, Masaya

AU - Nakagawa, Atsushi

AU - Ueda, Takuya

AU - Ochi, Kozo

AU - Higuchi, Yoshiki

N1 - Funding Information: We are grateful to Dr. N. Shimizu, Dr. M. Kawamoto and Dr. M. Yamamoto at SPring-8 for their help during data collection at synchrotron beamline BL41XU. This work was supported in part by Grants-in-Aid from the GCOE Programs (YH) and for Scientific Research from MEXT ( 18GS0207 ) (YH), 22370061 (YH), and 22657031 (YH), the Japanese Aerospace Exploration Agency Project (YH). We also thank the NBRP (NIG, Japan): E. coli for providing the ASKA clone (−) JW5873 used in this work.

PY - 2012/10/19

Y1 - 2012/10/19

N2 - The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3′,5′-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0 Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.

AB - The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3′,5′-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0 Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.

KW - GTPase

KW - Release factor

KW - Ribosome

KW - Stringent response

KW - Translation

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Crystal structure analysis of the translation factor RF3 (release factor 3)

Abstract

Keywords

ASJC Scopus subject areas

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