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PMID: 390500 Published · ppublish English Journal Article

Aspects of specific protein-DNA interaction; multi-mode binding of the oligopeptide antibiotic netropsin to (A.T)-rich DNA segments.

Nucleic acids research ·Vol. 7 ·No. 5 ·1979-11-10 ·Pages 1375-92

Reinert KE, Stutter E, Schweiss H

Abstract

By means of titration viscometry a number of distinct modes could be resolved for the interaction between the antibiotic netropsin and DNA species of 50, 58, and 69 mole + (A+T) below r = 0.04 netropsin molecules bound per DNA phosphate group. The number of corresponding binding sites increases with a high power of the (A+T) content. The apparent association constants are very high (greater than 10(6) M-1, some perhaps greater than 10(6) M-1) and also rather different for most of the binding sites. It is suggested that some of these interaction modes differ in the number of hydrogen bonds formed between donors of the ligand and acceptors of the binding sites. The interaction modes were characterized quantitatively by their (species-independent) changes of DNA contour length and by the percentage of local DNA stiffening.

MeSH Terms
Animals Binding Sites Cattle DNA Escherichia coli Guanidines Kinetics Mathematics Netropsin Nucleic Acid Conformation Poly dA-dT Polydeoxyribonucleotides Protein Binding Protein Conformation Temperature Thymus Gland Viscosity
Chemicals
Guanidines Polydeoxyribonucleotides Poly dA-dT Netropsin DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Reinert K E
Stutter E
Schweiss H
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40 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/7.5.1375
Published
1979-11-10
Pages
1375-92
Language
English
Region
England
NLM ID
0411011
PMCID
PMC342309
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/7.5.1375 PMC Full Text View journal details
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