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

L. A. Laimins, D. B. Rhoads, K. Altendorf, W. Epstein

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

The three structural proteins of the ATP-driven Kdp potassium transport system of E. coli has been identified and found to be located in the inner membrane. The high-affinity repressible Kdp system is one of 4 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.

Original languageEnglish (US)
Pages (from-to)3216-3219
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume75
Issue number7
DOIs
StatePublished - 1978

ASJC Scopus subject areas

  • General

Fingerprint

Dive into the research topics of 'Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli'. Together they form a unique fingerprint.

Cite this