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Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles

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Genes important for catalase activity in Enterococcus faecalis.

Michael Baureder¹, Lars Hederstedt

¹Microbiology Group, Department of Biology, Lund University, Lund, Sweden. Michael.Baureder@biol.lu.se

|May 17, 2012

Summary

This study identifies novel factors important for heme protein assembly in Enterococcus faecalis, revealing that the RNA degradosome and other genes are crucial for catalase (KatA) activity. These findings shed light on bacterial heme protein biogenesis.

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Area of Science:

Microbiology
Bacterial Physiology
Protein Biogenesis

Background:

Heme protein assembly in bacteria is not well understood.
Enterococcus faecalis synthesizes catalase (KatA) and cytochrome bd (CydAB) when provided with heme but does not produce heme itself.

Purpose of the Study:

To identify novel genes and factors involved in catalase biogenesis in E. faecalis.
To understand the mechanisms underlying heme protein assembly in this bacterium.

Main Methods:

Generation of E. faecalis gene insertion mutant libraries using transposons.
Screening of mutants for deficiencies in catalase activity via colony zymogram staining.
Analysis of identified genes and their roles in catalase expression.

Main Results:

Nine new genes, in addition to katA, were identified as important for catalase activity.
The RNA degradosome (srmB, rnjA), an ABC-type oligopeptide transporter (oppBC), a two-component signal transducer (etaR), and NADH peroxidase (npr) were implicated.
Catalase biogenesis was shown to be independent of CydABCD proteins.
A conserved proline in KatA's N-terminal region is vital for catalase assembly.

Conclusions:

The study identified key factors, including the RNA degradosome, essential for catalase activity in E. faecalis.
Catalase biogenesis is complex and involves multiple cellular components beyond the enzyme itself.
Specific protein features, like the N-terminal proline in KatA, are critical for proper protein assembly.