Conserved <i>C</i>-Terminal Tail Is Responsible for Membrane Localization and Function of <i>Pseudomonas aeruginosa</i> Hemerythrin.

ABSTRACT: Many bacteria have hemerythrin (Hr) proteins that bind O₂, including Pseudomonas aeruginosa, in which microoxia-induced Hr (Mhr) provide fitness advantages under microoxic conditions. Mhr has a 23 amino-acid extension at its C-terminus relative to a well-characterized Hr from Methylococcus capsulatus, and similar extensions are also found in Hrs from other bacteria. The last 11 amino acids of this extended, C-terminal tail are highly conserved in gammaproteobacteria and predicted to form a helix with positively charged and hydrophobic faces. In cellular fractionation assays, wild-type (WT) Mhr was found in both membrane and cytosolic fractions, while a Mhr^W143* variant lacking the last 11 residues was largely in the cytosol and did not comp

SUBMITTER: Stuut Balsam S 

PROVIDER: S-EPMC11481101 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature