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PMID: 356049 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 7 ·1978-07-00 ·Pages 3216-9

Laimins LA, Rhoads DB, Altendorf K, Epstein W

Abstract

The three structural proteins of the ATP-driven Kdp potassium transport system of Escherichia coli [Rhoads, D. B., Waters, F. B. & Epstein, W. (1976) J. Gen. Physiol. 67, 325-341] have been identified and found to be located in the inner membrane. The high-affinity repressible Kdp system in one of four potassium transport systems in E. coli. The Kdp proteins were identified both in growing cells as well as in heavily UV-irradiated cells infected with transducing phages carrying the kdp operon. Although all previously identified ATP-driven transport systems of Gram-negative bacteria have been shown to contain a periplasmic protein component, no evidence was found for such a component or for an outer membrane component of the Kdp system. The molecular weights of the three inner membrane proteins, KdpA, KdpB, and KdpC, were determined to be 47,000, 90,000 and 22,000, respectively.

MeSH Terms
Adenosine Triphosphate/metabolism Bacterial Proteins/genetics,metabolism Biological Transport, Active Cell Membrane/ultrastructure Coliphages Escherichia coli/genetics,metabolism Genes Membrane Proteins/genetics,metabolism Potassium/metabolism
Chemicals
Bacterial Proteins Membrane Proteins Adenosine Triphosphate Potassium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Laimins L A
Rhoads D B
Altendorf K
Epstein W
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26 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.7.3216
Published
1978-07-00
Pages
3216-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392745
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.7.3216 PMC Full Text View journal details
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