ArticleJournal of bacteriology2008
Functional differences between heme permeases: Serratia marcescens HemTUV permease exhibits a narrower substrate specificity (restricted to heme) than the Escherichia coli DppABCDF peptide-heme permease.
Article in Journal of bacteriology, 2008. 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, 23 citations in OpenAlex.
- Exceptional Heme Tolerance inLife (Basel, Switzerland) · 2025Article
- The modification of heme special importer to improve the production of active hemoglobins in Escherichia coli.Biotechnology letters · 2024Article
- Transcription regulation of iron carrier transport genes by ECF sigma factors through signaling from the cell surface into the cytoplasm.FEMS microbiology reviews · 2022Article
- Heme auxotrophy in abundant aquatic microbial lineages.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Serratia marcescens Siderophore Serratiochelin Is Necessary for Full Virulence during Bloodstream Infection.Infection and immunity · 2020Article
- Heme and hemoglobin utilization by Mycobacterium tuberculosis.Nature communications · 2019Article
- Article
- The iron-regulated staphylococcal lipoproteins.Frontiers in cellular and infection microbiology · 2012Review
- Heme utilization by nontypeable Haemophilus influenzae is essential and dependent on Sap transporter function.Journal of bacteriology · 2011Article
- Trafficking of heme and porphyrins in metazoa.Chemical reviews · 2009Review
- The dppBCDF gene cluster of Haemophilus influenzae: Role in heme utilization.BMC research notes · 2009Article
- Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serratia marcescens hemTUV genes encoding a potential heme permease were cloned in Escherichia coli recombinant mutant FB827 dppF::Km(pAM 238-hasR). This strain, which expresses HasR, a foreign heme outer membrane receptor, is potentially capable of using heme as an iron source. However, this process is invalidated due to a dppF::Km mutation which inactivates the Dpp heme/peptide permease responsible for heme, dipeptide, and delta-aminolevulinic (ALA) transport through the E. coli inner membrane. We show here that hemTUV genes complement the Dpp permease for heme utilization as an iron source and thus are functional in E. coli. However, hemTUV genes do not complement the Dpp permease for ALA uptake, indicating that the HemTUV permease does not transport ALA. Peptides do not inhibit heme uptake in vivo, indicating that, unlike Dpp permease, HemTUV permease does not transport peptides. HemT, the periplasmic binding protein, binds heme. Heme binding is saturable and not inhibited by peptides that inhibit heme uptake by the Dpp system. Thus, the S. marcescens HemTUV permease and, most likely, HemTUV orthologs present in many gram-negative pathogens form a class of heme-specific permeases different from the Dpp peptide/heme permease characterized in E. coli.
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