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• W1998466320 abstract "HetR plays a key role in regulation of heterocyst differentiation. When the Cys-48 residue of the HetR from Anabaena sp. PCC 7120 was replaced with an Ala residue, the mutant HetR (HetR(C48A)) could not dimerize, indicating that HetR forms a homodimer through a disulfide bond. The Anabaena strain C48, containing the hetRc48a gene, could not produce HetR homodimer and failed to form heterocyst. We show that HetR is a DNA-binding protein and that its homodimerization is required for the DNA binding. HetR binds the promoter regions of hetR, hepA, and patS, suggesting a direct control of the expression of these genes by HetR. We present evidence that shows that the up-regulation of patS and hetR depends on DNA binding by HetR dimer. The pentapeptide RGSGR, which is present at the C terminus of PatS and blocks heterocyst formation, inhibits the DNA binding of HetR and prevents hetR up-regulation." @default.
• W1998466320 created "2016-06-24" @default.
• W1998466320 creator A5051138632 @default.
• W1998466320 creator A5071502740 @default.
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• W1998466320 date "2004-03-29" @default.
• W1998466320 modified "2023-10-18" @default.
• W1998466320 title "HetR homodimer is a DNA-binding protein required for heterocyst differentiation, and the DNA-binding activity is inhibited by PatS" @default.
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• W1998466320 doi "https://doi.org/10.1073/pnas.0400429101" @default.
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