ArticleNucleic acids research2013
Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Drug resistance through ribosome splitting and rRNA disordering in mycobacteria.bioRxiv : the preprint server for biology · 2024Article
- Dual function of GTPBP6 in biogenesis and recycling of human mitochondrial ribosomes.Nucleic acids research · 2020Article
- Mycobacterial HflX is a ribosome splitting factor that mediates antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Impact of the Stringent Response on TRAFAC GTPases and Prokaryotic Ribosome Assembly.Cells · 2019Review
- Structural modules of the stress-induced protein HflX: an outlook on its evolution and biological role.Current genetics · 2019Review
- The universally conserved GTPase HflX is an RNA helicase that restores heat-damagedThe Journal of cell biology · 2018Article
- Disassembly of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- The putative Walker A and Walker B motifs of Rrp2 are required for the growth of Borrelia burgdorferi.Molecular microbiology · 2017Article
- Characterization of the autophosphorylation property of HflX, a ribosome-binding GTPase from Escherichia coli.FEBS open bio · 2016Article
- The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome.Nucleic acids research · 2016Article
- Novel MntR-independent mechanism of manganese homeostasis in Escherichia coli by the ribosome-associated protein HflX.Journal of bacteriology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A role for HflX in 50S-biogenesis was suggested based on its similarity to other GTPases involved in this process. It possesses a G-domain, flanked by uncharacterized N- and C-terminal domains. Intriguingly, Escherichia coli HflX was shown to hydrolyze both GTP and adenosine triphosphate (ATP), and it was unclear whether G-domain alone would explain ATP hydrolysis too. Here, based on structural bioinformatics analysis, we suspected the possible existence of an additional nucleotide-binding domain (ND1) at the N-terminus. Biochemical studies affirm that this domain is capable of hydrolyzing ATP and GTP. Surprisingly, not only ND1 but also the G-domain (ND2) can hydrolyze GTP and ATP too. Further; we recognize that ND1 and ND2 influence each other's hydrolysis activities via two salt bridges, i.e. E29-R257 and Q28-N207. It appears that the salt bridges are important in clamping the two NTPase domains together; disrupting these unfastens ND1 and ND2 and invokes domain movements. Kinetic studies suggest an important but complex regulation of the hydrolysis activities of ND1 and ND2. Overall, we identify, two separate nucleotide-binding domains possessing both ATP and GTP hydrolysis activities, coupled with an intricate inter-domain regulation for Escherichia coli HflX.
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