ASSIGNMENT OF THE H-1-NMR SPECTRUM OF A LAC REPRESSOR HEADPIECE-OPERATOR COMPLEX IN H2O AND IDENTIFICATION OF NOES - CONSEQUENCES FOR PROTEIN-DNA INTERACTION

RMJN LAMERICHS, R BOELENS, GA VANDERMAREL, JH VANBOOM, R KAPTEIN

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

A complex between the headpiece amino-terminal residues 1 - 56 of lac repressor (HP56) and an 11-bp lac operator fragment was studied by H-1 NMR. The sequence specific assignment of the exchangeable and nonexchangeable protons has been accomplished. Several protons have favourable chemical shifts in the complex, therefore new intraprotein NOEs could be found that had not been unambigously identified in the free protein. By comparison, most of these intraprotein NOEs are also present in the spectra of the free headpiece but some are different. Furthermore, several new protein DNA NOEs could be identified. The NOE between the side-chain amide protons of Gln18 and C5H of C7 confirms the specific contact between these residues which was proposed from genetic experiments [Ebright, R.M. (1985) J. Biomol. Struct. & Dyn. 3,281 - 297]. The implications of the new data for the interaction between the lac repressor headpiece and its operator are discussed.

Original languageEnglish
Pages (from-to)629-637
Number of pages9
JournalEuropean Journal of Biochemistry
Volume194
Issue number2
Publication statusPublished - 12 Dec 1990

Keywords

  • NUCLEAR MAGNETIC-RESONANCE
  • BINDING DOMAIN
  • TRP REPRESSOR
  • RESOLUTION
  • RECOGNITION
  • FRAGMENT
  • PROTON
  • LAMBDA
  • MOTIF
  • CRO

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