DNA-BINDING AND ENZYMATIC DOMAINS OF THE BIFUNCTIONAL BIOTIN OPERON REPRESSOR (BIRA) OF ESCHERICHIA-COLI
DNA-BINDING AND ENZYMATIC DOMAINS OF THE BIFUNCTIONAL BIOTIN OPERON REPRESSOR (BIRA) OF ESCHERICHIA-COLI
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DOI:
10.1016/0378-1119(86)90189-7
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发表时间:
1986-01-01
期刊:
影响因子:
3.5
通讯作者:
OTSUKA, AJ
中科院分区:
文献类型:
--
作者:
BUONCRISTIANI, MR;HOWARD, PK;OTSUKA, AJ
The negative regulation of the biotin biosynthetic (bio) operon in Escherichia coli is mediated by the bifunctional birA gene product, which serves as the bio repressor and biotin-activating enzyme. Nucleotide sequence analysis of 18 mutations in the birA gene was employed to study the DNA-binding and enzymatic functions of the BirA protein. The results indicate that a predicted helix-turn-helix structure, from amino acid (aa) positions 18 to 39 within the 321-aa BirA protein, may be responsible for sequence-specific DNA binding, whereas the temperature-sensitive mutations affecting biotin activation are found in two regions from aa positions 83-119 and 189-235.