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Nucleic Acids Research, 1977, Vol. 4, No. 11 3829-3838
© 1977

Articles

The binding of berenil to Escherichia coli ribosome*

S. Sinharay+, Z. Ali{ddagger} and D.P. Burma

Molecular Biology Unit, Department of Biochemistry, Institute of Medical Sciences, Banaras Hindu University Varanasi-221005, India

Received August 9, 1977.

The binding of the nonintercalating dye berenil to the 70S ribosome of Eacheriohia coli has been demonstrated by spectrophotometric measurements and gel filtration through Biogel P100 column. The berenil spectrum is gradually shifted towards the red region with the increasing amount of ribosome added, the isosbestic point being at 375 nm. There is positive cooperativity in the binding of berenil to the ribosome as demonstrated by the equilibrium dialysis. On binding with berenil, the ribosome is degraded faster by RNase I specially at low Mg++ concentration and its oapacity to inhibit RNase I catalysed hydrolysis of ribopolymers is decreased. These indicate the unfolding of the structure of the ribosome.

*The work was supported by the grants received by D.P.B. from the Council of Scientific and Industrial Research, New Delhi, the Department of Atomic Energy and the Department of Science and Technology, Government of India.

+Junior Research Fellow under a project sponsored by the Department of Atomic Energy, Government of India.

{dagger}Junior Research Fellow under a project sponsored by the Council of Scientific and Industrial Research, New Delhi.


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