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Journal article
Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein
The Journal Of Biological Chemistry, Vol.276, pp.2509-2516
276
2001
PMID: 11053417
Web of Science ID: WOS:000166784800030
Abstract
Bacteriophage T4 gene 32 protein, a model for singlestrand specific nucleic acid-binding proteins, consists of three structurally and functionally distinct domains. We have studied the effects of the N and C domains on the protein structure and its nucleic acid-interactive properties. Although the presence of the C domain decreases the proteolytic susceptibility of the core (central) domain, quenching of the core tryptophan fluorescence by iodide is unaltered by the presence of the terminal domains. These results suggest that the overall conformation of the core domain remains largely independent of the flanking domains. Removal of the N or the C terminus does not abolish the DNA renaturation activity of the protein. However, intact protein and its three truncated forms differ in DNA helix-destabilizing activity. The C domain alone is responsible for the kinetic barrier to natural DNA helix destabilization seen with intact protein. Intact protein and core domain potentiate the DNA helix-destabilizing activity of truncated protein lacking only the C domain (*I), enhancing the observed hyperchromicity while increasing the melting temperature. Proteolysis experiments suggest that the affinity of core domain for single-stranded DNA is increased in the presence of *I. We propose that *I can “mingle” with intact protein or core domain while bound to single-stranded DNA.
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Details
- Title
- Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein
- Publication Details
- The Journal Of Biological Chemistry, Vol.276, pp.2509-2516
- Resource Type
- Journal article
- Publisher
- American Society for Biochemistry and Molecular Biology, Inc.; Baltimore, MD
- Series
- 276
- Copyright
- 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
- Identifiers
- WOS:000166784800030; 99380090636106600
- Academic Unit
- Center for Environmental Diagnostics and Bioremediation ; Hal Marcus College of Science and Engineering ; Biology
- Language
- English