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TitleThe universally conserved GTPase HflX is an RNA helicase that restores heat-damaged ribosomes.
Journal, issue, pagesJ Cell Biol, Vol. 217, Issue 7, Page 2519-2529, Year 2018
Publish dateJul 2, 2018
AuthorsSandip Dey / Chiranjit Biswas / Jayati Sengupta /
PubMed AbstractThe 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.
External linksJ Cell Biol / PubMed:29930203 / PubMed Central
MethodsEM (single particle)
Resolution8.1 Å
Structure data

6979

5zzm

EMDB-6979, PDB-5zzm:
E. coli 50S subunit bound HflX protein in presence of ATP (AMP-PNP) and GTP (GMP-PNP) analogs.
Method: EM (single particle) / Resolution: 8.1 Å

Source
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsRIBOSOME / ATPase / RNA helicase / Heat stress

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