Biopolym. Cell. 1986; 2(2):106-111.
http://dx.doi.org/10.7124/bc.0001A4
Cell Biology
Specific interaction of the cro-repressor with operator site models. Circular dichroism studies
1Kirpichnikov M. P., 1Yartsev A. P., 1Minchenkova L. E., 1Chernov B. K., 1Ivanov V. I.
  1. Institute of Molecular Biology, Academy of Sciences of the USSR
    Moscow, USSR

Abstract

The circular dichroism (CD) method was used to study the interaction of the crorepressor of the phage A. with a synthetic OR3 operator of 17 base pairs long, and with its 9 base pairs fragment
5' TATCCCTT [GCGGTGATA]
3' ATAGGGAA [CGCCACTAT]
In both cases addition of cro-protein considerably changed the CD spectra in the region of 260-300 nm. The stoichiometry determined by the CD titration is identical both for OR3 and its fragment: one duplex per cro dimer. The interaction of the cro-protein with non-operator DNAs reveals no visible CD changes at all. The spectral changes during specific interaction are quite different from those for the B-A transition and for winding of the DNA within the B-family towards C-form. A conclusion is drawn that the CD changes are mainly induced by the CD effect in Tyr-26 during specific complex formation, the operator DNA conformation being conserved in a B-like form as a whole.
Full text: (PDF, in Russian)

References

[1] Richmond TJ, Finch JT, Rushton B, Rhodes D, Klug A. Structure of the nucleosome core particle at 7 A resolution. Nature. 1984 Oct 11-17;311(5986):532-7.
[2] Frederick CA, Grable J, Melia M, Samudzi C, Jen-Jacobson L, Wang BC, Greene P, Boyer HW, Rosenberg JM. Kinked DNA in crystalline complex with EcoRI endonuclease. Nature. 1984 May 24-30;309(5966):327-31.
[3] Culard F, Maurizot JC. Lac repressor - lac operator interaction. Circular dichroism study. Nucleic Acids Res. 1981;9(19):5175-84.
[4] Altschmied L, Hillen W. TET repressor.tet operator complex formation induces conformational changes in the tet operator DNA. Nucleic Acids Res. 1984;12(4):2171-80.
[5] Martin SR, Gronenborn AM, Clore GM. Specific DNA binding of the cyclic AMP receptor protein to a synthetic oligodeoxyribonucleotide. A circular dichroism study. FEBS Lett. 1983;159(1-2):102-6.
[6] Fried MG, Wu HM, Crothers DM. CAP binding to B and Z forms of DNA. Nucleic Acids Res. 1983;11(8):2479-94.
[7] Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. Structure of the cro repressor from bacteriophage lambda and its interaction with DNA. Nature. 1981;290(5809):754-8.
[8] Ohlendorf DH, Anderson WF, Fisher RG, Takeda Y, Matthews BW. The molecular basis of DNA-protein recognition inferred from the structure of cro repressor. Nature. 1982;298(5876):718-23.
[9] Kurochkin AV, Kirpichnikov MP. Studies of the structure of bacteriophage lambda cro protein in solution. Globular structure of cro protein. FEBS Lett. 1982;150(2):411-5.
[10] Bolotina IA, Kurochkin AV, Kirpichnikov MP. Studies of the structure of bacteriophage lambda cro protein in solution. Analysis of the circular dichroism data. FEBS Lett. 1983;155(2):291-4.
[11] Buck F, Tahn KD, Zemann W et al. NMR-study of repressor-operator interactions. Proc. fifth intern, symp. metabolism and enzymology nucl. acids including gene manipulations. Bratislava, 1984:27-40.
[12] Ivanov VI, Minchenkova LE, Shchelkina AK, Chernou BK, Yartsev AP, Kirpichnikov MP. Conformation of the OR3 operator of phage and its fragment in aqueous and aqueous-trifluoroethanol solutions. Biopolym. Cell. 1986; 2(2):101-6.
[13] Kirpichnikov MP, Hahn KD, Buck F, RГјterjans H, Chernov BK, Kurochkin AV, Skryabin KG, Bayev AA. 1H NMR study of the interaction of bacteriophage lambda Cro protein with the OR3 operator. Evidence for a change of the conformation of the OR3 operator on binding. Nucleic Acids Res. 1984;12(8):3551-61.
[14] Roberts TM, Kacich R, Ptashne M. A general method for maximizing the expression of a cloned gene. Proc Natl Acad Sci U S A. 1979;76(2):760-4.
[15] Kirpichnikov MP, Kurochkin AV, Skryabin KG. Studies of the structure of bacteriophage lambda cro protein in solution. Analysis of the aromatic region of the 1H NMR spectrum. FEBS Lett. 1982;150(2):407-10.