Secondary Structure of the Lac Repressor DNA-binding Domain by Two-dimensional 1H Nuclear Magnetic Resonance in Solution

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1983 Oct 1

PMID 6351066

Citations 12

Authors

E R Zuiderweg

R Kaptein

K Wuthrich

Affiliations

Soon will be listed here.

Abstract

A recently proposed approach for spatial structure determination in noncrystalline proteins by nuclear magnetic resonance was applied to the lac repressor DNA-binding domain. On the basis of sequence-specific 1H NMR assignments, the location of alpha-helices in the amino acid sequence was determined from nuclear Overhauser enhancement data and from amide proton exchange studies. These investigations provide detailed experimental data on the structure of a noncrystalline DNA-binding protein. The results support the hypothesis advanced by others that sequence-specific interactions between lac repressor and DNA are mediated by a particular spatial arrangement of two alpha-helices common to various different DNA-binding proteins.

Citing Articles

Introduction to a special issue of in honour of Robert Kaptein at the occasion of his 80th birthday.

Boelens R, Ivanov K, Matysik J Magn Reson (Gott). 2023; 2(1):465-474.

PMID: 37904778 PMC: 10539797. DOI: 10.5194/mr-2-465-2021.

Graph-theoretical assignment of secondary structure in multidimensional protein NMR spectra: application to the lac repressor headpiece.

Slijper M, Boelens R, Kaptein R J Biomol NMR. 1995; 6(1):67-78.

PMID: 7663143 DOI: 10.1007/BF00417493.

A model for the non-specific binding of catabolite gene activator protein to DNA.

Weber I, Steitz T Nucleic Acids Res. 1984; 12(22):8475-87.

PMID: 6390343 PMC: 320391. DOI: 10.1093/nar/12.22.8475.

Dynamic filtering by two-dimensional 1H NMR with application to phage lambda repressor.

Weiss M, Eliason J, States D Proc Natl Acad Sci U S A. 1984; 81(19):6019-23.

PMID: 6237367 PMC: 391850. DOI: 10.1073/pnas.81.19.6019.

Lac repressor-Lac operator complexes. Solution X-ray scattering and electrophoretic studies.

Culard F, Charlier M, Maurizot J, Tardieu A Eur Biophys J. 1987; 14(3):169-78.

PMID: 3549272 DOI: 10.1007/BF00253842.

References

HVIDT A, Nielsen S . Hydrogen exchange in proteins. Adv Protein Chem. 1966; 21:287-386. DOI: 10.1016/s0065-3233(08)60129-1. View

Wuthrich K . Sequential individual resonance assignments in the 1H-nmr spectra of polypeptides and proteins. Biopolymers. 1983; 22(1):131-8. DOI: 10.1002/bip.360220121. View

Geisler N, Weber K . Isolation of amino-terminal fragment of lactose repressor necessary for DNA binding. Biochemistry. 1977; 16(5):938-43. DOI: 10.1021/bi00624a020. View

Buck F, Ruterjans H, Beyreuther K . 1H NMR study of the lactose repressor from Escherichia coli. FEBS Lett. 1978; 96(2):335-8. DOI: 10.1016/0014-5793(78)80430-x. View

Wade-Jardetzky N, Bray R, Conover W, Jardetzky O, Geisler N, Weber K . Differential mobility of the N-terminal headpiece in the lac-repressor protein. J Mol Biol. 1979; 128(2):259-64. DOI: 10.1016/0022-2836(79)90129-3. View

Miller J, Coulondre C, Hofer M, Schmeissner U, Sommer H, Schmitz A . Genetic studies of the lac repressor. IX. Generation of altered proteins by the suppression of nonsence mutations. J Mol Biol. 1979; 131(2):191-222. DOI: 10.1016/0022-2836(79)90073-1. View

Ogata R, Gilbert W . DNA-binding site of lac repressor probed by dimethylsulfate methylation of lac operator. J Mol Biol. 1979; 132(4):709-28. DOI: 10.1016/0022-2836(79)90384-x. View

Buck F, Ruterjans H, Kaptein R, Beyreuther K . Photochemically induced dynamic nuclear polarization investigation of complex formation of the NH2-terminal DNA-binding domain of lac repressor with poly[d(AT)]. Proc Natl Acad Sci U S A. 1980; 77(9):5145-8. PMC: 350013. DOI: 10.1073/pnas.77.9.5145. View

Ribeiro A, Wemmer D, Bray R, Jardetzky O . High-resolution nuclear magnetic resonance studies of the Lac repressor. 1. Assignments of tyrosine resonances in the N-terminal headpiece. Biochemistry. 1981; 20(4):818-23. DOI: 10.1021/bi00507a025. View

10.

Ribeiro A, Wemmer D, Bray R, Jardetzky O . High-resolution nuclear magnetic resonance studies of the Lac repressor. 2. Partial analysis of the aliphatic region of the Lac repressor headpiece spectrum. Biochemistry. 1981; 20(4):823-9. DOI: 10.1021/bi00507a026. View

11.

Wemmer D, Ribeiro A, Bray R, Jardetzky O . High-resolution nuclear magnetic resonance studies of the Lac repressor. 3. Unfolding of the Lac repressor headpiece. Biochemistry. 1981; 20(4):829-33. DOI: 10.1021/bi00507a027. View

12.

Braun W, Bosch C, Brown L, Go N, Wuthrich K . Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon. Biochim Biophys Acta. 1981; 667(2):377-96. DOI: 10.1016/0005-2795(81)90205-1. View

13.

McKay D, Steitz T . Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA. Nature. 1981; 290(5809):744-9. DOI: 10.1038/290744a0. View

14.

Anderson W, Ohlendorf D, Takeda Y, Matthews B . Structure of the cro repressor from bacteriophage lambda and its interaction with DNA. Nature. 1981; 290(5809):754-8. DOI: 10.1038/290754a0. View

15.

Nagayama K . Two-dimensional NMR spectroscopy: an application to the study of flexibility of protein molecules. Adv Biophys. 1981; 14:139-204. View

16.

Ribeiro A, Wemmer D, Bray R, Jardetzky O . A folded structure for the lac-repressor headpiece. Biochem Biophys Res Commun. 1981; 99(2):668-74. DOI: 10.1016/0006-291x(81)91796-4. View

17.

Ribeiro A, Wemmer D, Bray R, Jardetzky O . pH dependence of the high-resolution proton nuclear magnetic resonance spectrum of the lac repressor headpiece. Biochemistry. 1981; 20(12):3346-50. DOI: 10.1021/bi00515a005. View

18.

Wemmer D, Shvo H, Ribeiro A, Bray R, Jardetzky O . High-resolution proton nuclear magnetic resonance studies of the exchangeable resonances of the lac repressor headpiece. Biochemistry. 1981; 20(12):3351-4. DOI: 10.1021/bi00515a006. View

19.

Arndt K, Boschelli F, Lu P, Miller J . lac Repressor: a proton magnetic resonance look at the deoxyribonucleic acid binding fragment. Biochemistry. 1981; 20(21):6109-18. DOI: 10.1021/bi00524a030. View

20.

Matthews B, Ohlendorf D, Anderson W, Takeda Y . Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor. Proc Natl Acad Sci U S A. 1982; 79(5):1428-32. PMC: 345986. DOI: 10.1073/pnas.79.5.1428. View