TRAAK is an ion channel from the two-pore domain potassium (K
2P
) channel family with roles in maintaining the resting membrane potential and fast action potential conduction. Regulated by a wide range of physical and chemical stimuli, the affinity and selectivity of K
2P
4.1 towards lipids remains poorly understood. Here we show the two isoforms of K
2P
4.1 have distinct binding preferences for lipids dependent on acyl chain length and position on the glycerol backbone. Unexpectedly, the channel can also discriminate the fatty acid linkage at the
sn
-1 position. Of the 33 lipids interrogated using native mass spectrometry, phosphatidic acid (PA) had the lowest equilibrium dissociation constants for both isoforms of K
2P
4.1. Liposome potassium flux assays with K
2P
4.1 reconstituted in defined lipid environments show that those containing PA activate the channel in a dose-dependent fashion. Our results begin to define the molecular requirements for the specific binding of lipids to K
2P
4.1.
Achromobacter spp. are ubiquitous Gram-negative bacteria, some of which can cause respiratory tract infections in patients with autoimmune disorders and cystic fibrosis. Bacteriophages have therapeutic and biotechnological potential to combat Achromobacter sp. infections. This announcement details the 42.5-kb genome sequence of the temperate Achromobacter xylosoxidans myophage Mano.
Stenotrophomonas maltophilia
is emerging as an opportunistic multidrug-resistant pathogen.
S. maltophilia
podophage Philippe has a 74,717-bp genome which is related broadly to the N4-like phage group, including
Stenotrophomonas
phage Pokken. The low sequence identity to other described phages suggests that Philippe is an unclassified member of the N4-like subfamily
Rothmandenesvirinae
.
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