DNA-Binding Activity of Amino-Terminal Domains of the Bacillus subtilis AbrB Protein
| Autor: | Mark A. Strauch, Ke Xu |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Binding Sites
biology Protein Conformation fungi Amino Acid Motifs Genetics and Molecular Biology Bacillus subtilis Plasma protein binding biology.organism_classification Microbiology DNA-binding protein Peptide Fragments DNA-Binding Proteins Protein structure Bacterial Proteins Biochemistry Binding site Molecular Biology Transcription factor Peptide sequence Protein Binding Transcription Factors Cysteine |
| Zdroj: | Journal of Bacteriology. 183:4094-4098 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.183.13.4094-4098.2001 |
| Popis: | Two truncated variants of AbrB, comprising either its first 53 (AbrBN53) or first 55 (AbrBN55) amino acid residues, were constructed and purified. Noncovalently linked homodimers of the truncated variants exhibited very weak DNA-binding activity. Cross-linking AbrBN55 dimers into tetramers and higher-order multimers (via disulfide bonding between penultimate cysteine residues) resulted in proteins having DNA-binding affinity comparable to and DNA-binding specificity identical to those of intact, wild-type AbrB. These results indicate that the DNA recognition and specificity determinants of AbrB binding lie solely within its N-terminal amino acid sequence. |
| Databáze: | OpenAIRE |
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