A Periplasmic Lanthanide Mediator, Lanmodulin, in Methylobacterium aquaticum Strain 22A.

ABSTRACT: Methylobacterium and Methylorubrum species oxidize methanol via pyrroloquinoline quinone-methanol dehydrogenases (MDHs). MDHs can be classified into two major groups, Ca²⁺-dependent MDH (MxaF) and lanthanide (Ln³⁺)-dependent MDH (XoxF), whose expression is regulated by the availability of Ln³⁺. A set of a siderophore, TonB-dependent receptor, and an ABC transporter that resembles the machinery for iron uptake is involved in the solubilization and transport of Ln³⁺. The transport of Ln³⁺ into the cytosol enhances XoxF expression. A unique protein named lanmodulin from Methylorubrum extorquens strain AM1 was identified as a specific Ln³⁺-binding protein, and its biological function was implicated to

SUBMITTER: Fujitani Y 

PROVIDER: S-EPMC9260416 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature