However, we demonstrate that it is also able to recognize an atypical operator site by binding as a dimer-of-dimers and the extended N-terminal regions of ArtA were shown to be essential for this dimer-of-dimer binding mode. Strikingly, unlike most well-studied RHH proteins ArtA binds its cognate operators as a dimer. The structure reveals that ArtA is representative of a new family of ribbon–helix–helix (RHH) DNA-binding proteins that contain extended, N-terminal basic motifs. To elucidate the mechanism by which it specifically recognizes its DNA site, we obtained the structure of ArtA bound to its cognate operator, ACATGACATG. ArtA shows no sequence homology to any structurally characterized DNA-binding protein. aureus multi-resistance plasmid pSK41 is a global transcriptional regulator of pSK41 genes, including those involved in conjugation and segregation. Here, we demonstrate that the ArtA protein encoded by the S. Plasmid conjugation and partition are critical to the dissemination and inheritance of such plasmids. Plasmids harbored by Staphylococcus aureus are a major contributor to the spread of bacterial multi-drug resistance.
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