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Abstract
The first identification of an inverted repeat motif within the AcrIF11-Aca7 operon promoter from Halomonas caseinilytica was reported.
- Aca7 protein specifically binds to the identified inverted repeat element in the operon promoter.
- Structural analysis shows Aca7 forms a symmetric dimer that interacts with both major grooves of the DNA.
- The binding of Aca7 stabilizes DNA bending through contacts in the minor groove.
- Key amino acids (R38, Q42, K46, and K49) are involved in the sequence-specific recognition of the DNA.
- Distinct differences in dimer architecture and DNA deformation strategies were observed when comparing Aca2 and Aca7.
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