ArticleJournal of bacteriology2006
Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Exceptional Heme Tolerance inLife (Basel, Switzerland) · 2025Article
- An Exposed Outer Membrane Hemin-Binding Protein Facilitates Hemin Transport by a TonB-Dependent Receptor in Riemerella anatipestifer.Applied and environmental microbiology · 2021Article
- Extracellular haem utilization by the opportunistic pathogen Pseudomonas aeruginosa and its role in virulence and pathogenesis.Advances in microbial physiology · 2021Article
- Post-transcriptional regulation of theThe Journal of biological chemistry · 2019Article
- Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.The Biochemical journal · 2016Article
- Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans.Frontiers in cellular and infection microbiology · 2013Review
- Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Bacterial heme-transport proteins and their heme-coordination modes.Archives of biochemistry and biophysics · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cells sense the extracellular environment and adapt to that environment by activating gene regulation circuits, often by means of signaling molecules. The Serratia marcescens hemophore is a signaling molecule that acts as an extracellular heme-scavenging protein. The heme-loaded hemophore interacts with its cognate receptor (HasR), triggering transmembrane signaling and turning on transcription of hemophore-dependent heme uptake genes. We investigated the features of the holo-hemophore, the only HasR ligand known to act as an inducer. We used a hemophore mutant that does not deliver its heme and a HasR mutant that does not bind heme, and we showed that heme transfer from the hemophore to the receptor is necessary for induction. Using a hemophore mutant that does not bind heme and that blocks heme transport, we demonstrated that two molecules that do not interact (heme and the mutant hemophore) may nonetheless induce this system. These findings suggest that hemophore-mediated induction and heme transport involve different mechanisms. The hemophore region important for induction was precisely localized to amino acids 50 to 55, which lie in one of the two HasR-binding hemophore regions. This bipartite stimulus probably corresponds to a physiological process because heme is transferred to the receptor before apo-hemophore release. This bipartite regulation mechanism may allow the bacterium to adjust its heme transport mechanism to the perceived environmental heme concentration.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.