FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2042026122> ?p ?o ?g. }

• W2042026122 endingPage "16487" @default.
• W2042026122 startingPage "16477" @default.
• W2042026122 abstract "Iron is an essential nutrient for the proliferation of Staphylococcus aureus during bacterial infections. The iron-regulated surface determinant (Isd) system of S. aureus transports and metabolizes iron porphyrin (heme) captured from the host organism. Transportation of heme across the thick cell wall of this bacterium requires multiple relay points. The mechanism by which heme is physically transferred between Isd transporters is largely unknown because of the transient nature of the interactions involved. Herein, we show that the IsdC transporter not only passes heme ligand to another class of Isd transporter, as previously known, but can also perform self-transfer reactions. IsdA shows a similar ability. A genetically encoded photoreactive probe was used to survey the regions of IsdC involved in self-dimerization. We propose an updated model that explicitly considers self-transfer reactions to explain heme delivery across the cell wall. An analogous photo-cross-linking strategy was employed to map transient interactions between IsdC and IsdE transporters. These experiments identified a key structural element involved in the rapid and specific transfer of heme from IsdC to IsdE. The resulting structural model was validated with a chimeric version of the homologous transporter IsdA. Overall, our results show that the ultra-weak interactions between Isd transporters are governed by bona fide protein structural motifs. Iron is an essential nutrient for the proliferation of Staphylococcus aureus during bacterial infections. The iron-regulated surface determinant (Isd) system of S. aureus transports and metabolizes iron porphyrin (heme) captured from the host organism. Transportation of heme across the thick cell wall of this bacterium requires multiple relay points. The mechanism by which heme is physically transferred between Isd transporters is largely unknown because of the transient nature of the interactions involved. Herein, we show that the IsdC transporter not only passes heme ligand to another class of Isd transporter, as previously known, but can also perform self-transfer reactions. IsdA shows a similar ability. A genetically encoded photoreactive probe was used to survey the regions of IsdC involved in self-dimerization. We propose an updated model that explicitly considers self-transfer reactions to explain heme delivery across the cell wall. An analogous photo-cross-linking strategy was employed to map transient interactions between IsdC and IsdE transporters. These experiments identified a key structural element involved in the rapid and specific transfer of heme from IsdC to IsdE. The resulting structural model was validated with a chimeric version of the homologous transporter IsdA. Overall, our results show that the ultra-weak interactions between Isd transporters are governed by bona fide protein structural motifs." @default.
• W2042026122 created "2016-06-24" @default.
• W2042026122 creator A5024778748 @default.
• W2042026122 creator A5045077292 @default.
• W2042026122 creator A5049932117 @default.
• W2042026122 creator A5072979871 @default.
• W2042026122 creator A5078386276 @default.
• W2042026122 date "2012-05-01" @default.
• W2042026122 modified "2023-10-15" @default.
• W2042026122 title "Mapping Ultra-weak Protein-Protein Interactions between Heme Transporters of Staphylococcus aureus" @default.
• W2042026122 cites W1523166866 @default.
• W2042026122 cites W1834847254 @default.
• W2042026122 cites W1969290393 @default.
• W2042026122 cites W1974311793 @default.
• W2042026122 cites W1975256163 @default.
• W2042026122 cites W1977289330 @default.
• W2042026122 cites W1979135961 @default.
• W2042026122 cites W1982899294 @default.
• W2042026122 cites W1986826865 @default.
• W2042026122 cites W1989272792 @default.
• W2042026122 cites W1995265717 @default.
• W2042026122 cites W1998120501 @default.
• W2042026122 cites W2001366878 @default.
• W2042026122 cites W2034065930 @default.
• W2042026122 cites W2035503835 @default.
• W2042026122 cites W2036727331 @default.
• W2042026122 cites W2038391169 @default.
• W2042026122 cites W2040874215 @default.
• W2042026122 cites W2043624646 @default.
• W2042026122 cites W2045029351 @default.
• W2042026122 cites W2050965833 @default.
• W2042026122 cites W2063482352 @default.
• W2042026122 cites W2066341000 @default.
• W2042026122 cites W2067344044 @default.
• W2042026122 cites W2075153401 @default.
• W2042026122 cites W2075521951 @default.
• W2042026122 cites W2076913495 @default.
• W2042026122 cites W2078429251 @default.
• W2042026122 cites W2079754673 @default.
• W2042026122 cites W2080638771 @default.
• W2042026122 cites W2086399987 @default.
• W2042026122 cites W2086406020 @default.
• W2042026122 cites W2094045382 @default.
• W2042026122 cites W2094950664 @default.
• W2042026122 cites W2101871915 @default.
• W2042026122 cites W2109542969 @default.
• W2042026122 cites W2123293956 @default.
• W2042026122 cites W2125814033 @default.
• W2042026122 cites W2126383924 @default.
• W2042026122 cites W2129535039 @default.
• W2042026122 cites W2132629607 @default.
• W2042026122 cites W2134749398 @default.
• W2042026122 cites W2150923940 @default.
• W2042026122 cites W2155310008 @default.
• W2042026122 cites W2156502117 @default.
• W2042026122 cites W2163053334 @default.
• W2042026122 cites W2168482920 @default.
• W2042026122 cites W2169346900 @default.
• W2042026122 cites W2314649741 @default.
• W2042026122 cites W2329427515 @default.
• W2042026122 cites W2330065888 @default.
• W2042026122 cites W266512168 @default.
• W2042026122 cites W88967424 @default.
• W2042026122 doi "https://doi.org/10.1074/jbc.m112.346700" @default.
• W2042026122 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3351326" @default.
• W2042026122 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22427659" @default.
• W2042026122 hasPublicationYear "2012" @default.
• W2042026122 type Work @default.
• W2042026122 sameAs 2042026122 @default.
• W2042026122 citedByCount "44" @default.
• W2042026122 countsByYear W20420261222012 @default.
• W2042026122 countsByYear W20420261222013 @default.
• W2042026122 countsByYear W20420261222014 @default.
• W2042026122 countsByYear W20420261222015 @default.
• W2042026122 countsByYear W20420261222016 @default.
• W2042026122 countsByYear W20420261222017 @default.
• W2042026122 countsByYear W20420261222018 @default.
• W2042026122 countsByYear W20420261222019 @default.
• W2042026122 countsByYear W20420261222020 @default.
• W2042026122 countsByYear W20420261222021 @default.
• W2042026122 countsByYear W20420261222022 @default.
• W2042026122 countsByYear W20420261222023 @default.
• W2042026122 crossrefType "journal-article" @default.
• W2042026122 hasAuthorship W2042026122A5024778748 @default.
• W2042026122 hasAuthorship W2042026122A5045077292 @default.
• W2042026122 hasAuthorship W2042026122A5049932117 @default.
• W2042026122 hasAuthorship W2042026122A5072979871 @default.
• W2042026122 hasAuthorship W2042026122A5078386276 @default.
• W2042026122 hasBestOaLocation W20420261221 @default.
• W2042026122 hasConcept C104317684 @default.
• W2042026122 hasConcept C12554922 @default.
• W2042026122 hasConcept C149011108 @default.
• W2042026122 hasConcept C181199279 @default.
• W2042026122 hasConcept C185592680 @default.
• W2042026122 hasConcept C2776217839 @default.
• W2042026122 hasConcept C2779480358 @default.
• W2042026122 hasConcept C2779489039 @default.
• W2042026122 hasConcept C523546767 @default.

• next