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Journal of Biochemistry Advance Access published online on December 15, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm238
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© 2007 The Japanese Biochemical Society

Rapid Communication

Interdomain interaction of cyclic AMP receptor protein in the absence of cyclic AMP

Hyung-Sik Won1,*, Min-Duk Seo2, Hyun-Suk Ko1, Wahn Soo Choi3 and Bong-Jin Lee2,{dagger}

1Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-70; 2Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742; and 3Department of Immunology, College of Medicine, Konkuk University, Chungju, Chungbuk 380-701, Korea

*To whom correspondence should be addressed. Dr. Won, Hyung-Sik, Tel: +82-43-840-3589, Fax: +82-43-852-3616, E-mail: wonhs@kku.ac.kr

{dagger}Correspondence may also be addressed. Tel: +82-2-880-7869, Fax: +82-2-872-3632, E-mail: lbj{at}nmr.snu.ac.kr

Received November 6, 2007; Accepted November 30, 2007


  Abstract

Interdomain interaction of apo-cyclic AMP receptor protein (apo-CRP) was qualified using its isolated domains. The cAMP-binding domain was prepared by a limited proteolysis, while the DNA-binding domain was constructed as a recombinant protein. Three different regions making interdomain contacts in apo-CRP were identified by a sequence-specific comparison of the HSQC spectra. The results indicated that apo-CRP possesses characteristic modules of interdomain interaction that are properly organized to suppress activity and to sense and transfer the cAMP binding signals. Particularly, the inertness of the DNA-binding motif in apo-CRP was attributable to the participation of F-helices in the interdomain contacts.

Key Words: allostery, cyclic AMP receptor protein, heteronuclear single quantum coherence, interdomain interaction, nuclear magnetic resonance


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