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PMID: 140863 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Normal iron-enterochelin uptake in mutants lacking the colicin I outer membrane receptor protein of Escherichia coli.

Journal of bacteriology ·Vol. 130 ·No. 3 ·1977-06-00 ·Pages 1399-401

Soucek S, Konisky J

Abstract

The outer membranes of two independent colicin Ia-resistant mutants of Escherichia coli K-12 lack the colicin Ia receptor protein. Such mutants exhibit normal capacity for enterochelin (enterobactin)-mediated iron uptake. It is concluded that the colicin Ia receptor is not involved in iron-enterochelin uptake.

MeSH Terms
Bacterial Proteins/metabolism Colicins/metabolism Drug Resistance, Microbial Enterobactin/metabolism Escherichia coli/metabolism Iron/metabolism Membrane Proteins/metabolism Mutation Protein Binding Receptors, Drug/metabolism Serine/analogs & derivatives
Chemicals
Bacterial Proteins Colicins Membrane Proteins Receptors, Drug Enterobactin Serine Iron
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Soucek S
Konisky J
References (16)
16 references, click to expand
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  5. The role of colicin receptors in the uptake of ferrienterochelin by Escherichia coli K-12.
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    J Bacteriol. 1972 Dec;112(3):1142-9 PMID: 4565531
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    J Bacteriol. 1971 Oct;108(1):553-63 PMID: 5001205
  14. The colicin I receptor of Escherichia coli K-12 has a role in enterochelin-mediated iron transport.
    FEBS Lett. 1976 Jun 1;65(2):208-10 PMID: 776694
  15. Iron transport of Escherichia coli K-12: involvement of the colicin B receptor and of a citrate-inducible protein.
    J Bacteriol. 1976 Sep;127(3):1370-5 PMID: 783142
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1977-06-00
Pages
1399-401
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC235374
Subset
IM
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