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Journal of Bacteriology, July 2001, p. 4094-4098, Vol. 183, No. 13
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.13.4094-4098.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

DNA-Binding Activity of Amino-Terminal Domains of the Bacillus subtilis AbrB Protein

Ke Xu^1, and Mark A. Strauch^2,*

Division of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037,¹ and Department of Oral and Craniofacial Biological Sciences, University of MarylandBaltimore, Baltimore, Maryland 21201²

Received 5 January 2001/Accepted 30 March 2001

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.

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^* Corresponding author. Mailing address: Department of Oral and Craniofacial Biological Sciences, University of MarylandBaltimore, 666 W. Baltimore St., Baltimore, MD 21201. Phone: (410) 706-1815. Fax: (410) 706-0865. E-mail: mas002{at}dental.umaryland.edu.

Present address: Global Research and Development, Pfizer, Inc., Groton, CT 06340.

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Journal of Bacteriology, July 2001, p. 4094-4098, Vol. 183, No. 13
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.13.4094-4098.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

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