Functional Characterization of the γ-Aminobutyric Acid Transporter from Mycobacterium smegmatis MC² 155 Reveals Sodium-Driven GABA Transport.

ABSTRACT: Characterizing the mycobacterial transporters involved in the uptake and/or catabolism of host-derived nutrients required by mycobacteria may identify novel drug targets against tuberculosis. Here, we identify and characterize a member of the amino acid-polyamine-organocation superfamily, a potential γ-aminobutyric acid (GABA) transport protein, GabP, from Mycobacterium smegmatis The protein was expressed to a level allowing its purification to homogeneity, and size exclusion chromatography coupled with multiangle laser light scattering (SEC-MALLS) analysis of the purified protein showed that it was dimeric. We showed that GabP transported γ-aminobutyric acid both in vitro and when overexpressed in E. coli Additionally, transport was greatly reduced in the presence of

SUBMITTER: Pavic A 

PROVIDER: S-EPMC7847548 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature