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-Structure paper
タイトル | The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged ribosomes. |
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ジャーナル・号・ページ | J Cell Biol, Vol. 217, Issue 7, Page 2519-2529, Year 2018 |
掲載日 | 2018年7月2日 |
著者 | Sandip Dey / Chiranjit Biswas / Jayati Sengupta / |
PubMed 要旨 | The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Although HflX is recognized as a guanosine triphosphatase, ...The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Although HflX is recognized as a guanosine triphosphatase, several studies have shown that the N-terminal domain 1 of HflX is capable of hydrolyzing adenosine triphosphate (ATP), but the functional role of its adenosine triphosphatase (ATPase) activity remains unknown. We demonstrate that HflX possesses ATP-dependent RNA helicase activity and is capable of unwinding large subunit ribosomal RNA. A cryo-electron microscopy structure of the 50S-HflX complex in the presence of nonhydrolyzable analogues of ATP and guanosine triphosphate hints at a mode of action for the RNA helicase and suggests the linker helical domain may have a determinant role in RNA unwinding. Heat stress results in inactivation of the ribosome, and we show that HflX can restore heat-damaged ribosomes and improve cell survival. |
リンク | J Cell Biol / PubMed:29930203 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 8.1 Å |
構造データ | |
由来 |
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キーワード | RIBOSOME / ATPase / RNA helicase / Heat stress |