Structural highlights
Function
[HFLX_ECOLI] GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. In vitro, also exhibits ATPase activity.[HAMAP-Rule:MF_00900][1] [2] [3]
Publication Abstract from PubMed
The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Escherichia coli 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 E. coli 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.
The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes.,Dey S, Biswas C, Sengupta J J Cell Biol. 2018 Jul 2;217(7):2519-2529. doi: 10.1083/jcb.201711131. Epub 2018, Jun 21. PMID:29930203[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jain N, Dhimole N, Khan AR, De D, Tomar SK, Sajish M, Dutta D, Parrack P, Prakash B. E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides. Biochem Biophys Res Commun. 2009 Feb 6;379(2):201-5. doi:, 10.1016/j.bbrc.2008.12.072. Epub 2008 Dec 25. PMID:19109926 doi:http://dx.doi.org/10.1016/j.bbrc.2008.12.072
- ↑ Dutta D, Bandyopadhyay K, Datta AB, Sardesai AA, Parrack P. Properties of HflX, an enigmatic protein from Escherichia coli. J Bacteriol. 2009 Apr;191(7):2307-14. doi: 10.1128/JB.01353-08. Epub 2009 Jan 30. PMID:19181811 doi:http://dx.doi.org/10.1128/JB.01353-08
- ↑ Shields MJ, Fischer JJ, Wieden HJ. Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: a kinetic approach. Biochemistry. 2009 Nov 17;48(45):10793-802. doi: 10.1021/bi901074h. PMID:19824612 doi:http://dx.doi.org/10.1021/bi901074h
- ↑ Dey S, Biswas C, Sengupta J. The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes. J Cell Biol. 2018 Jul 2;217(7):2519-2529. doi: 10.1083/jcb.201711131. Epub 2018, Jun 21. PMID:29930203 doi:http://dx.doi.org/10.1083/jcb.201711131
