Fos and Jun Do Not Bend the AP-1 Recognition Site

We have used a solution-based DNA cyclization assay and a gel-phasing method to show that contrary to previous reports [Kerppola, T. K. & Curran, T. (1991) Cell 66, 317-326], basic region leucine zipper proteins Fos and Jun do not significantly bend their AP-1 recognition site. We have construct...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1996-04, Vol.93 (8), p.3248-3252
Hauptverfasser: Sitlani, Ayesha, Crothers, Donald M.
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Sprache:eng
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Zusammenfassung:We have used a solution-based DNA cyclization assay and a gel-phasing method to show that contrary to previous reports [Kerppola, T. K. & Curran, T. (1991) Cell 66, 317-326], basic region leucine zipper proteins Fos and Jun do not significantly bend their AP-1 recognition site. We have constructed two sets of DNA constructs that contain the 7-bp 5′-TGACTCA-3′ AP-1 binding site, from either the yeast or the human collagenase gene, which is well separated from and phased by 3-4 helical turns against an A tract-directed bend. The cyclization probabilities of DNAs with altered phasings are not significantly affected by Fos-Jun binding. Similarly, Fos-Jun and Jun-Jun bound to differently phased DNA constructs show insignificant variations in gel mobilities. Both these methods independently indicate that Fos and Jun bend their AP-1 target site by
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.93.8.3248