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Science 13 February 1987:
Vol. 235. no. 4790, pp. 777 - 780
DOI: 10.1126/science.3027895

Articles

Science, Vol 235, Issue 4790, 777-780
Copyright © 1987 by American Association for the Advancement of Science


articles

Synthesis of a site-specific DNA-binding peptide

MF Bruist, SJ Horvath, LE Hood, TA Steitz, and MI Simon

The Hin recombinase binds to specific sites on DNA and mediates a recombination event that results in DNA inversion. In order to define the DNA-binding domain of the Hin protein two peptides 31 and 52 amino acids long were synthesized. Even though the 31mer encompassed the sequence encoding the putative helix-coil-helix-binding domain, it was not sufficient for binding to the 26-base pair DNA crossover site. However, the 52mer specifically interacted with the site and also effectively inhibited the Hin-mediated recombination reaction. The 52mer bound effectively to both the 26-base pair complete site and to a 14-base pair "half site." Nuclease and chemical protection studies with the 52mer helped to define the DNA base pairs that contributed to the specificity of binding. The synthetic peptide provides opportunities for new approaches to the study of the nature of protein-DNA interaction.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions.
J. Feng, R. Johnson, and R. Dickerson (1994)
Science 263, 348-355
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Zinc-dependent structure of a single-finger domain of yeast ADR1.
G Parraga, S. Horvath, A Eisen, W. Taylor, L Hood, E. Young, and R. Klevit (1988)
Science 241, 1489-1492
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Phase variation in Salmonella: analysis of Hin recombinase and hix recombination site interaction in vivo..
K T Hughes, P Youderian, and M I Simon (1988)
Genes & Dev. 2, 937-948
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Biotechnology and Medicine of the Future.
L. Hood (1988)
JAMA 259, 1837-1844
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Synthesis of a sequence-specific DNA-cleaving peptide.
J. Sluka, S. Horvath, M. Bruist, M. Simon, and P. Dervan (1987)
Science 238, 1129-1132
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Sequence-specific cleavage of double helical DNA by triple helix formation.
H. Moser and P. Dervan (1987)
Science 238, 645-650
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The C-peptide Helix from Ribonuclease A Considered as an Autonomous Folding Unit.
K.R. Shoemaker, R. Fairman, P.S. Kim, E.J. York, J.M. Stewart, and R.L. Baldwin (1987)
Cold Spring Harb Symp Quant Biol 52, 391-398
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