Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 74, Issue 5, Pages 1145-1151Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2009.09.024
Keywords
Aurintricarboxylic acid; Telomerase; DNase I; RNase A; Reverse transcriptase; Taq polymerase; Tryptophan fluorescence; Circular dichroism
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Funding
- Department of Science and Technology (DST), Government of India
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In the investigation of interaction of aurintricarboxylic acid (ATA) with four biologically important proteins we observed inhibition of enzymatic activity of DNase I, RNase A, M-MLV reverse transcriptase and Taq polymerase by ATA in vitro assay. As the telomerase reverse transcriptase (TERT) is the main catalytic subunit of telomerase holoenzyme, we also monitored effect of ATA on telomerase activity in vivo and observed dose-dependent inhibition of telomerase activity in Chinese hamster V79 cells treated with ATA. Direct association of ATA with DNase I (K-d = 9.019 mu M)), RNase A (K-d = 2.33 mu M) reverse transcriptase (K-d = 0.255 mu M) and Taq polymerase (K-d = 81.97 mu M) was further shown by tryptophan fluorescence quenching studies. Such association altered the three-dimensional conformation of DNase I, RNase A and Taq polymerase as detected by circular dichroism. We propose ATA inhibits enzymatic activity of the four proteins through interfering with DNA or RNA binding to the respective proteins either competitively or allosterically, i.e. by perturbing three-dimensional structure of enzymes. (C) 2009 Elsevier B.V. All rights reserved.
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