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Nucleic Acids Research, 1990, Vol. 18, No. 6 1457-1464
© 1990

MOLECULAR BIOLOGY

Lysine 188 of the catabolite gene activator protein (CAP) plays no role in specificity at base pair 7 of the DNA half site

Richard H. Ebright*, Angelo Gunasekera, Xiaoping Zhang, Thomas A. Kunkel1 and Joseph S. Krakow2

Department of Chemistry and Waksman Institute, Rutgers University New Brunswick, NJ 08855 1 NIH-NIEHS Research Triangle Park, NC 27709 2Department of Biology, Hunter College of CUNY New York, NY 10021, USA

*To whom correspondence should be addressed

Received December 11, 1989. Revised February 21, 1990. Accepted February 21, 1990.

Two similar, but not identical, models have been proposed for the amino acid-base pair contacts in the CAP-DNA complex (‘model I,’ Weber, I. and Steitz, T., Proc. Natl. Acad. Sci. USA, 81, 3973–3977, 1984; ‘model II,’ Ebright, et al., Proc. Natl. Acad. Sci. USA, 81, 7274–7278, 1984). The most important difference between the two models involves Lys188 of CAP. Model I predicts that Lys188 of CAP makes a specificity determining contact with base pair 7 of the DNA half site. In contrast, model II predicts that Lys188 makes no contact with base pair 7 of the DNA half site. In the present work, we have used site-directed mutagenesis to replace Lys188 of CAP by Asn, an amino acid unable to make the putative contact. We have assessed the specificities of the following proteins, both in vitro and in vivo: wild-type CAP, [Asn188]CAP, [Val181]CAP and [Val181;Asn188]CAP. The results indicate that Lys188 makes no contribution to specificity at base pair 7 of the DNA half site. We propose, contrary to model I, that Lys188 makes no contact with base pair 7 of the DNA half site.


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