ArticleMolecular microbiology2020
One evolutionarily selected amino acid variation is sufficient to provide functional specificity in the cold shock protein paralogs of Staphylococcus aureus.
Article in Molecular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 16 citations in OpenAlex.
- Identification of proteins influencing CRISPR-associated transposases for enhanced genome editing.Science advances · 2026Article
- Article
- An internal loop region is responsible for inherent target specificity of bacterial cold-shock proteins.RNA (New York, N.Y.) · 2024Article
- Natural variation of immune epitopes reveals intrabacterial antagonism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Overlapping and Distinct Functions of the Paralogous PagR Regulators of Bacillus anthracis.Journal of bacteriology · 2022Article
- TMT proteomic analysis for molecular mechanism of Staphylococcus aureus in response to freezing stress.Applied microbiology and biotechnology · 2022Article
- Regulation of Heterogenous LexA Expression inInternational journal of molecular sciences · 2022Article
- Functional Redundancy and Specialization of the Conserved Cold Shock Proteins inMicroorganisms · 2021Article
- Review
- RNA thermoswitches modulate Staphylococcus aureus adaptation to ambient temperatures.Nucleic acids research · 2021Article
- Review
- One evolutionarily selected amino acid variation is sufficient to provide functional specificity in the cold shock protein paralogs of Staphylococcus aureus.Molecular microbiology · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial genomes encode several families of protein paralogs. Discrimination between functional divergence and redundancy among paralogs is challenging due to their sequence conservation. Here, we investigated whether the amino acid differences present in the cold shock protein (CSP) paralogs of Staphylococcus aureus were responsible for functional specificity. Since deletion of cspA reduces the synthesis of staphyloxanthin (STX), we used it as an in vivo reporter of CSP functionality. Complementation of a ΔcspA strain with the different S. aureus CSP variants showed that only CspA could specifically restore STX production by controlling the activity of the stress-associated sigma B factor (σ
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