Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend.

Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Research Abstract Details 

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Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Abstract Text:

BACKGROUND: Proteins can force DNA to adopt distorted helical structures that are rarely if ever observed in naked DNA. The ability to synthesize DNA that contains defined helical aberrations would offer a new avenue for exploring the structural and energetic plasticity of DNA. Here we report a strategy for the enforcement of non-canonical helical structures through disulfide cross-linking; this approach is exemplified by the design and synthesis of an oligonucleotide containing a pronounced bend. RESULTS: A localized bend was site-specifically introduced into DNA by the formation of a disulfide cross-link between the 5' adenines of a 5'-AATT-3' region in complementary strands of DNA. The DNA bend was characterized by high-resolution NMR structure determination of a cross-linked dodecamer and electrophoretic mobility assays on phased multimers, which together indicate that the cross-linked tetranucleotide induces a helical bend of approximately 30 degrees and a modest degree of unwinding. The enforced bend was found to stimulate dramatically the binding of an architecture-specific protein, HMG-D, to the DNA. DNase I foot-printing analysis revealed that the protein is recruited to the section of DNA that is bent. CONCLUSIONS: The present study reports a novel approach for the investigation of non-canonical DNA structures and their recognition by architecture-specific proteins. The mode of DNA bending induced by disulfide cross-linking resembles that observed in structures of protein-DNA complexes. The results reveal common elements in the DNA-binding mode employed by sequence-specific and architecture-specific HMG proteins.

Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Publishing Authors By Initials

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Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Chemistry & biology

VOLUME: 2

Page Numbers: 213-21

Journal Abbreviation: Chem. Biol.

ISSN: 1074-5521

DAY: 13

MONTH: Apr

YEAR: 1995

Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Information

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LANGUAGE: eng

NlmUniqueID: 9500160

Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Information

Substance Name: Deoxyribonuclease I

Registry Number: EC 3.1.21.1

Grant and Affiliation Information for Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend.

AFFILIATION: Department of Chemistry, Harvard University, Cambridge, MA 02138, USA.

Country: ENGLAND

AGENCY: United States NCRR

GRANT: P41 RR005964-070020

ACRONYM: RR

MEDLINETA: Chem Biol

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