Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 279, Issue 45, Pages 47076-47080Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C400417200
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Funding
- NHLBI NIH HHS [HL54171, R01 HL054171] Funding Source: Medline
- NIDDK NIH HHS [K08 DK060086, DK60086] Funding Source: Medline
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The Kir gene family encodes inward rectifying K+ ( Kir) channels that are widespread and critical regulators of excitability in eukaryotic cells. A related gene family (KirBac) has recently been identified in prokaryotes. While a crystal structure of one member, KirBac1.1, has been solved, there has been no functional characterization of any KirBac gene products. Here we present functional characterization of KirBac1.1 reconstituted in liposomes. Utilizing a Rb-86(+) uptake assay, we demonstrate that KirBac1.1 generates a K+-selective permeation path that is inhibited by extraliposomal Ba2+ and Ca2+ ions. In contrast to KcsA ( an acid-activated bacterial potassium channel), KirBac1.1 is inhibited by extraliposomal acid (pK(a) similar to 6). This characterization of KirBac1.1 activity now paves the way for further correlation of structure and function in this model Kir channel.
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