Metabolic Sensing of Extracytoplasmic Copper Availability via Translational Control by a Nascent Exported Protein

Öztürk, Yavuz; Andrei, Andreea; Blaby-Haas, Crysten E.; Daum, Noel; Daldal, Fevzi; Koch, Hans‐Georg; Johnson, ed.

doi:10.1128/mbio.03040-22

Cited by 5 publications

(3 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result suggests that the function of RAPP-containing arrest peptides is not limited to the regulation of the Sec or YidC pathway. In accordance with this notion, recent studies have suggested that the CruR and CutF uORFs, which harbor RAPP and polyproline sequences, respectively, play roles in regulating the downstream ORFs encoding the TonB-dependent transporter BfrG and multicopper oxidase CutO, respectively 43,44 , although the translation arrest of either of them has yet to be demonstrated experimentally.…”

Section: Discussionmentioning

confidence: 91%

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

Fujiwara,

Tsuji,

Yoshida

et al. 2023

Preprint

View full text Add to dashboard Cite

Regulatory arrest peptides exert cellular functions via mechanisms involving regulated translational arrest. Monitoring substrates, a class of arrest peptides, feedback-regulate the expression of the Sec or YidC protein localization machinery. Previously, only a limited number of monitoring substrates were identified. In this study, we performed a bacterial domain-wide search, followed byin vivoandin vitroanalyses, leading to a comprehensive identification of many novel Sec/YidC-related arrest peptides that showed patchy, but widespread, phylogenetic distribution throughout the bacterial domain. Identification of five novel arrest-inducing sequences suggests that bacteria have evolved various arrest-inducing mechanisms. We also identified many arrest peptides that share an R-A-P-P like sequence, suggesting that this sequence could serve as a common evolutionary seed that could overcome the species-specific structures of ribosomes, to evolve arrest peptides. Our comprehensive phylogenetic study revealed that arrest peptide is a prevalent mechanism for the gene regulation of the protein localization machinery.

show abstract

Section: Discussionmentioning

confidence: 91%

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

Fujiwara,

Tsuji,

Yoshida

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

“…This result suggests that the function of RAPP-containing arrest peptides is not limited to the regulation of the Sec or YidC pathway. In accordance with this notion, recent studies have suggested that the CruR and CutF uORFs, which harbor RAPP and poly-proline sequences, respectively, play roles in regulating the downstream ORFs encoding the TonB-dependent transporter BfrG and multicopper oxidase CutO, respectively 47 , 48 , although the translation arrest of either of them has yet to be demonstrated experimentally.…”

Section: Discussionmentioning

confidence: 91%

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

Fujiwara,

Tsuji,

Yoshida

et al. 2024

Nat Commun

View full text Add to dashboard Cite

Regulatory arrest peptides interact with specific residues on bacterial ribosomes and arrest their own translation. Here, we analyse over 30,000 bacterial genome sequences to identify additional Sec/YidC-related arrest peptides, followed by in vivo and in vitro analyses. We find that Sec/YidC-related arrest peptides show patchy, but widespread, phylogenetic distribution throughout the bacterial domain. Several of the identified peptides contain distinct conserved sequences near the C-termini, but are still able to efficiently stall bacterial ribosomes in vitro and in vivo. In addition, we identify many arrest peptides that share an R-A-P-P-like sequence, suggesting that this sequence might serve as a common evolutionary seed to overcome ribosomal structural differences across species.

show abstract

“…However, copper also has toxic effects on cells, and bacteria have several strategies to increase their resistance to copper 20,21 . The direct bacterial response associated with copper resistance is highly conserved and generally involves (a) sensing of the increased copper concentration by sensors, (b) activation of bespoke transcriptional networks, (c) overproduction of copper efflux pumps that secrete copper out of the cells, and (d) recruitment of copper-binding and copper-oxidizing proteins that prevent copper from interacting with cellular components [22][23][24][25][26] . In addition to the above copper resistance strategies, bacteria can avoid copper stress through chemotaxis.…”

Section: Introductionmentioning

confidence: 99%

Coordinated regulation of chemotaxis and resistance to copper by CsoR inPseudomonas putida

He,

Tao,

et al. 2024

Preprint

View full text Add to dashboard Cite

Copper is an essential enzyme cofactor in bacteria, but excess copper is highly toxic. Bacteria can cope with copper stress by increasing copper resistance and initiating chemorepellent response. However, it remains unclear how bacteria coordinate chemotaxis and resistance to copper. By screening proteins that interacted with the chemotaxis kinase CheA, we identified a copper-binding repressor CsoR that interacted with CheA inPseudomonas putida. CsoR interacted with the HPT (P1), Dimer (P3), and HATPase_c (P4) domains of CheA and inhibited CheA autophosphorylation, resulting in decreased chemotaxis. The copper-binding of CsoR weakened its interaction with CheA, which relieved the inhibition of chemotaxis by CsoR. In addition, CsoR bound to the promoter of copper-resistance genes to inhibit gene expression, and copper-binding released CsoR from the promoter, leading to increased gene expression and copper resistance.P. putidacells exhibited a chemorepellent response to copper in a CheA-dependent manner, and CsoR inhibited the chemorepellent response to copper. Besides, the CheA-CsoR interaction also existed in proteins from several other bacterial species. Our results revealed a mechanism by which bacteria coordinately regulated chemotaxis and resistance to copper by CsoR.

show abstract

Metabolic Sensing of Extracytoplasmic Copper Availability via Translational Control by a Nascent Exported Protein

Abstract: Metabolite sensing is a fundamental biological process, and the perception of dynamic changes in the extracellular environment is of paramount importance for the survival of organisms. Bacteria usually adjust their metabolisms to changing environments via transcriptional regulation.

Cited by 5 publications

References 70 publications

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

Coordinated regulation of chemotaxis and resistance to copper by CsoR inPseudomonas putida

Contact Info

Product

Resources

About