A structure-function study of ZraP and ZraS provides new insights into the two-component system Zra

• Published in: Biochimica et biophysica acta. General subjects Vol. 1865; no. 3; p. 129810
• Main Authors: Taher, Raleb, de Rosny, Eve
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2021; Elsevier
• Subjects: Amino Acid Sequence; Arabinose - chemistry; Arabinose - metabolism; atomic absorption spectrometry; Binding Sites; Biochemistry, Molecular Biology; circular dichroism spectroscopy; Cloning, Molecular; crosslinking; Crystallography, X-Ray; cysteine; Envelope stress response; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; fluorescence; Gene Expression Regulation, Bacterial; Genetic Vectors - chemistry; Genetic Vectors - metabolism; histidine kinase; homeostasis; Life Sciences; Models, Molecular; Periplasm - genetics; Periplasm - metabolism; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Multimerization; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; small-angle X-ray scattering; stress response; Structural Biology; Structure-Activity Relationship; toxicity; Trans-Activators - chemistry; Trans-Activators - genetics; Trans-Activators - metabolism; Two-component systems; X-radiation; zinc; Zinc - chemistry; Zinc - metabolism; Zinc binding proteins; Zra system; ZraP; ZraS; ZraS; Zinc binding proteins; Two-component systems; ZraP; Envelope stress response; Zra system

Zra belongs to the envelope stress response (ESR) two-component systems (TCS). It is atypical because of its third periplasmic repressor partner (ZraP), in addition to its histidine kinase sensor protein (ZraS) and its response regulator (ZraR) components. Furthermore, although it is activated by Zn...