Genetic and physiological regulation of intrinsic proteins of the outer membrane of Salmonella typhimurium

Bennett, Robert L.; Rothfield, Lawrence

doi:10.1128/jb.127.1.498-504.1976

Cited by 35 publications

(9 citation statements)

References 18 publications

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“…A similar pattern was observed in outer membrane protein profiles from iron-starved fluorescent pseudomonads (25). Iron starvation also leads to the appearance of several highmolecular-weight proteins in outer membranes of enteric bacteria (6,7,16,18,19,24,29).…”

Section: Discussionsupporting

confidence: 72%

Energy-independent uptake of iron from citrate by isolated outer membranes of Neisseria meningitidis

Simonson¹,

Trivett²,

DeVoe³

1981

Infect Immun

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Cyanide-poisoned Neisseria meningitidis SD1C cells rapidly took up 'Fe from iron-citrate complexes during the first 2 min, after which no further iron was accumulated. ['4C]citrate was not taken up concomitantly with 'Fe by these cells.The 'Fe taken up by the poisoned cells was found in the membrane fraction after cells were broken; 70% of the radioactivity was distributed in the outer membrane, and 30% was in the inner membrane. Isolated outer membranes from iron-starved cells were as capable of iron uptake from citrate as intact cells were. As with whole cells, ['4C]citrate was not taken up by isolated outer membranes. A polyacrylamide gel electrophoresis analysis of the proteins from citrate-dialyzed outer membranes after the uptake of 'Fe revealed that the radioactivity was associated with a major band of 36,500 molecular weight.Other recent evidence has shown that meningococci can use human transferrin-bound iron as t Permanent address: Department of Biology, Pacific Union College, Angwin CA 94508. 50 ng of ferrous ammonium sulfate per ml (final concentration) to a final optical density at 600 nm of 0.3 (model 250 spectrophotometer; Gilford Instrument Laboratories, Ontario, Canada). A 75-ml volume of this suspension was the inoculum for 1,425 ml of NDM.The final culture medium contained less than 10 ng of Fe per ml as contaminating iron before inoculation.Cultures in this iron-limited medium (Fig. 1) were incubated at 37°C, in 5% CO2 in air until division in 547 on August 3, 2020 by guest http://iai.asm.org/ Downloaded from

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Section: Discussionsupporting

confidence: 72%

Energy-independent uptake of iron from citrate by isolated outer membranes of Neisseria meningitidis

Simonson¹,

Trivett²,

DeVoe³

1981

Infect Immun

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“…Recently, Williams (20) described another iron uptake system mediated by the ColV plasmid of invasive Escherichia coli strains of human and animal origin. This system is independent of the enterochelin system of iron uptake described for enteric bacteria (1,15).…”

Section: Discussionmentioning

confidence: 95%

Outer membrane proteins induced under conditions of iron limitation in the marine fish pathogen Vibrio anguillarum 775

Crosa¹,

Hodges²

1981

Infect Immun

113

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Cells of the marine fish pathogen Vibrio anguillarum 775 harboring a plasmid associated with virulence can grow unaffected in the presence of iron-binding compounds such as transferrin. In contrast, the growth of isogenic plasmidless derivatives is inhibited by the presence of iron chelators. Radioactive iron ('Fe3") uptake experiments indicate that this plasmid-linked ability of V. anguillarum cells to grow under conditions of iron limitation is indeed due to a more rapid and efficient iron uptake mediated by the virulence plasmid. In addition, V. anguillarum cells growing under iron limitation show at least two novel outer membrane proteins. One of them, a 86,000-dalton protein we called OM2, is inducible only in those cells in which the virulence plasmid is present.

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“…It has been shown previously that growth in low-iron medium induces the appearance of enzymes responsible for synthesis of enterochelin and for degradation of iron-enterochelin complexes (5,28), synthesis of component(s) responsible for uptake of iron-enterochelin complexes by intact cells 16, and synthesis of a group of iron-repressible major outer-membrane proteins (1,3,12,25). The present paper adds to this list the uptake of ferrichrome by intact cells, a finding consistent with the studies of Negrin and Neilands on ferrichrome uptake in inner-membrane vesicles of E. coli (26).…”

Section: Discussionmentioning

confidence: 99%

“…Thus, growth in lqw-iron medium induces the appearance of enzymes responsible for synthesis of enterochelin (5,25) and for intracellular degradation of iron-enterochelin complexes (29) and also i assocated with a significant increase in cellular uptake of ironenterochelin (16). In addition, growth in lowiron medium is asociated with the appearance ofthree outer-membrane proteins, referred to as OM1, OM2, and OM3 in S. typhinwrm (1) and…”

mentioning

confidence: 99%

Constitutive expression of the iron-enterochelin and ferrichrome uptake systems in a mutant strain of Salmonella typhimurium

Ernst¹,

Bennett²,

Rothfield³

1978

J Bacteriol

Self Cite

160

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Two hih-affinity iron uptake systems are known in Salmonella typhunurinum, one utiig iron-enteohelin and the other uliing ferichrome. It has been shown previously that expreon of several element of the iron-enterochelin uptake system are ated by the iron content of the medium, with growth in high-iron medium resulting in repon of enzymes of enterochelin synthsis and degradation and of the ability of whole cels to take up iron-enterochelin In this study we describe a mutant strain in which growth in high-iron medium was assciated with constitutive exreon of. (i) iron-enterochelin uptake by whole cells (ii) ferirome uptake by whole cells; (iii) synthesis of enterochelin; (iv) itracellular degradation of iron-enterochelin; and (v) synthesis of three major outer-membe prot (OM1, OM2, and OM3). In conbwtr in the wildtype strain the4s prorties were only after growth in iron-deficient medium. It is proposed that the mutation ffects a gene responsible for regulating expssion of the structual genes for the components of the high-affinity iron uptake ystems. The term fur, for iron (Fe) uptake regulation, is suggetd for this new class of mutant. Several high-affinity systems are known to perticipate in iron uptake in SabnoneUa typhimurinum and Ewcherichia coli. The enterochelin uptake system facilitates entry of iron complexed to enterochelin, a cyclic trimer of 2,3dihydroxybenzoylserine syntheized and excreted by the bacterium itself. This presumably represents the physiologically relevant system under most circunutances (3, 31). The fernchrome uptake system facilitates entry of iron complexed to siderophores produced by fimgi (3, 19, 23). A third high-affinity uptake systm facilitats entry ofiron-citrate complexes in E. coli but is not present in S. typhimurium (8, 32).

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Genetic and physiological regulation of intrinsic proteins of the outer membrane of Salmonella typhimurium

Cited by 35 publications

References 18 publications

Energy-independent uptake of iron from citrate by isolated outer membranes of Neisseria meningitidis

Energy-independent uptake of iron from citrate by isolated outer membranes of Neisseria meningitidis

Outer membrane proteins induced under conditions of iron limitation in the marine fish pathogen Vibrio anguillarum 775

Constitutive expression of the iron-enterochelin and ferrichrome uptake systems in a mutant strain of Salmonella typhimurium

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