Promoted evolution of a shortened variant of heme A synthase in the membrane of Bacillus subtilis

• Published in: FEBS letters Vol. 582; no. 9; pp. 1330 - 1334
• Main Authors: Lewin, Anna, Hederstedt, Lars
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 16.04.2008
• Subjects: Amino Acid Sequence; Bacillus subtilis; Bacillus subtilis - enzymology; Bacillus subtilis - genetics; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Base Sequence; Biochemistry and Molecular Biology; Biokemi och molekylärbiologi; Biologi; Biological Evolution; Biological Sciences; Cell Membrane - enzymology; CtaA; Cytochrome a; Cytochrome b Group - chemistry; Cytochrome b Group - genetics; Cytochrome b Group - metabolism; DNA Primers; Electrophoresis, Polyacrylamide Gel; Gene Deletion; Heme A synthesis; Membrane protein evolution; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Proteins - metabolism; Microbiology; Mikrobiologi; Molecular Sequence Data; Natural Sciences; Naturvetenskap; CtaA; Cytochrome a; Heme A synthesis; Bacillus subtilis; Membrane protein evolution
• ISSN: 0014-5793; 1873-3468; 1873-3468
• DOI: 10.1016/j.febslet.2008.03.015

Bacillus subtilis heme A synthase is a membrane protein with 8 transmembrane segments. By using a two-step mutagenesis approach we have generated and selected a fully functional enzyme protein variant with a seven residue internal deletion. The biochemical properties of the shortened variant are similar to those of the normal enzyme. This could indicate that residue H209 in the mutant protein substitutes for the missing H216 as an axial ligand to the heme iron. Our results provide insight in routes of membrane protein evolution and the structure of heme A synthases.