HflX protein protects Escherichia coli from manganese stress

Sengupta, Sandeepan; Mondal, Avisek; Dutta, Dipak; Parrack, Pradeep

doi:10.1007/s12038-018-9807-9

Cited by 8 publications

(7 citation statements)

References 40 publications

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“…HflX is under control of heat-induced promoters in the superoperon and has been demonstrated to be a heat-shock protein (Carruthers and Minion, 2009; Chuang and Blattner, 1993; Zhang et al, 2015). HflX was also reported to involve in cellular responses to osmotic and hypoxic stresses (Ngan et al, 2021; Weber et al, 2006), and participates in the regulation of the manganese homeostasis in E. coli (Kaur et al, 2014; Sengupta et al, 2018). These data, together with the experiment results that HflX mediates different antibiotic resistance in different bacterial species (Fig.…”

Section: Discussionmentioning

confidence: 99%

Cryo-EM Structure of the 50S-HflX Complex Reveals a Novel Mechanism of Antibiotic Resistance inE. coli

Dai

Gao

2022

Preprint

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Bacterial HflX is a conserved ribosome-binding GTPase involved in splitting ribosomal complexes accumulated under stress condition. However, the atomic details of its ribosomal interaction remain to be elucidated. In this work, we present a high-resolution structure of the E. coli 50S subunit bound with HflX. The structure reveals highly specific contacts between HflX and the ribosomal RNA, and in particular, an insertion loop of the N-terminal domain of HflX is situated in the peptidyl transferase center (PTC) and makes direct interactions with PTC residues. Interestingly, this loop displays steric clash with a few PTC-targeting antibiotics on the 50S subunit, such as chloramphenicol. Deletion of hflX results in hypersensitivity to chloramphenicol treatment, and a loop residue G154 of HflX is important for the observed chloramphenicol resistance. Overall, our results suggest that HflX could be a general stress response factor that functions in both stalled ribosome splitting and PTC antibiotic displacing.

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Section: Discussionmentioning

confidence: 99%

Cryo-EM Structure of the 50S-HflX Complex Reveals a Novel Mechanism of Antibiotic Resistance inE. coli

Dai

Gao

2022

Preprint

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“…3). Similarly we were unable to detect increased sensitivity to excess manganese, another phenotype observed in E. coli HflX mutants (Kaur et al, 2014;Sengupta et al, 2018). This suggests that Arabidopsis HflX is not involved in chloroplast ribosome rescue or manganese homeostasis under the conditions tested, or that HflX plays a redundant role that can be replaced by other factors.…”

Section: Discussionmentioning

confidence: 67%

“…In E. coli, hflx mutants are also hypersensitive to excess manganese, a stress characterized by growth arrest, filamentation and lower rates of replication (Kaur et al, 2014; Sengupta et al, 2018). Therefore, we investigated the effect of excessive manganese on the growth of hflx mutants by germinating seeds on a medium supplemented with 2mM Mn 2+ or on control plates without manganese.…”

Section: Resultsmentioning

confidence: 99%

Insights into the function of the chloroplastic ribosome-associated GTPase HflX inArabidopsis thaliana

Mehrez

Lecampion

et al. 2023

Preprint

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Ribosome-associated GTPases are conserved enzymes that participate in ribosome biogenesis and ribosome function. In bacteria, recent studies have identified HflX as a ribosome-associated GTPase that is involved in both ribosome biogenesis and recycling under stress conditions. Plants possess a chloroplastic HflX homolog, but its function remains unknown. Here, we characterised the role of HflX in the plantArabidopsis thaliana. Our findings demonstrate that HflX does not have a detectable role in plant growth and development, nor does it play a distinct role in acclimation to several different stresses, including heat, manganese, cold, and salt stress. However, we found that HflX is required for plant resistance to chloroplast translational stress mediated by the antibiotic lincomycin. Our results suggest that HflX is a chloroplast ribosome-associated protein that may play a role in the surveillance of translation. These findings provide new insight into the function of HflX as a ribosome-associated GTPase in plants and highlight the importance of investigating conserved proteins in different organisms to gain a comprehensive understanding of their biological roles.

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“…The chemicals and concentrations tested are listed in Table 1 . These concentrations were chosen based on a literature search to find MIC values determined by other studies [ 30 , 35 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 ]. Based on these results ( Figure S1 ), we chose the following concentrations for the subsequent experiments: 0.2 mM NaAsO 2 , 2.0 mM CuSO 4 , 0.2 mM CdSO 4 , 5.0 mM MnCl 2 , and 0.37 mM ZnCl 2 .…”

Section: Resultsmentioning

confidence: 99%

The Effect of Heavy Metals on Conjugation Efficiency of an F-Plasmid in Escherichia coli

et al. 2022

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Conjugation, the process by which conjugative plasmids are transferred between bacteria, is regarded as a major contributor to the spread of antibiotic resistance, in both environmental and clinical settings. Heavy metals are known to co-select for antibiotic resistance, but the impact of the presence of these metals on conjugation itself is not clear. Here, we systematically investigate the impact that five heavy metals (arsenic, cadmium, copper, manganese, and zinc) have on the transfer of an IncF conjugative plasmid in Escherichia coli. Our results show that two of the metals, cadmium and manganese, have no significant impact, while arsenic and zinc both reduce conjugation efficiency by approximately 2-fold. Copper showed the largest impact, with an almost 100-fold decrease in conjugation efficiency. This was not mediated by any change in transcription from the major Py promoter responsible for transcription of the conjugation machinery genes. Further, we show that in order to have this severe impact on the transfer of the plasmid, copper sulfate needs to be present during the mating process, and we suggest explanations for this.

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HflX protein protects Escherichia coli from manganese stress

Cited by 8 publications

References 40 publications

Cryo-EM Structure of the 50S-HflX Complex Reveals a Novel Mechanism of Antibiotic Resistance inE. coli

Cryo-EM Structure of the 50S-HflX Complex Reveals a Novel Mechanism of Antibiotic Resistance inE. coli

Insights into the function of the chloroplastic ribosome-associated GTPase HflX inArabidopsis thaliana

The Effect of Heavy Metals on Conjugation Efficiency of an F-Plasmid in Escherichia coli

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