Additivity in protein-DNA interactions: How good an approximation is it?

Panayiotis V. Benos, Martha L. Bulyk, Gary D. Stormo

Research output: Contribution to journalArticlepeer-review

262 Scopus citations

Abstract

Man and Stormo and Bulyk et al. recently presented their results on the study of the DNA binding affinity of proteins. In both of these studies the main conclusion is that the additivity assumption, usually applied in methods to search for binding sites, is not true. In the first study, the analysis of binding affinity data from the Mnt repressor protein bound to all possible DNA (sub)targets at positions 16 and 17 of the binding site, showed that those positions are not independent. In the second study, the authors analysed DNA binding affinity data of the wild-type mouse EGR1 protein and four variants differing on the middle finger. The binding affinity of these proteins was measured to all 64 possible trinucleotide (sub)targets of the middle finger using microarray technology. The analysis of the measurements also showed interdependence among the positions in the DNA target. In the present report, we review the data of both studies and we reanalyse them using various statistical methods, including a comparison with a multiple regression approach. We conclude that despite the fact that the additivity assumption does not fit the data perfectly, in most cases it provides a very good approximation of the true nature of the specific protein-DNA interactions. Therefore, additive models can be very useful for the discovery and prediction of binding sites in genomic DNA.

Original languageEnglish
Pages (from-to)4442-4451
Number of pages10
JournalNucleic acids research
Volume30
Issue number20
DOIs
StatePublished - Oct 15 2002

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