Abstract
The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) is an acidic protein of 84 amino acids that inactivates uracil-DNA glycosylase from diverse organisms (Wang, Z., and Mosbaugh, D. W. (1989) J. Biol. Chem. 264, 1163-1171). The secondary structure of Ugi has been determined by solution state multidimensional nuclear magnetic resonance. The protein adopts a single well defined structure consisting of five anti-parallel beta-strands and two alpha-helices. Six loop or turn regions were identified that contain approximately one half of the acidic amino acid residues and connect the beta-strands sequentially to one another. The secondary structure suggests which regions of Ugi may be involved in interactions with uracil-DNA glycosylase.
Highlights
Uracil residues may be introduced into DNA by the incorporation of dUMP during DNA synthesis or by the deamination of cytosine in DNA
The nuclear magnetic resonance (NMR) spectrometer was purchased with support from National Science Foundation BIR 93-03077
Uracil residues located in the herpes simplex 1 origin of replication (Oris) hamper specific recognition by the origin binding protein [24], and inactivation of the vaccinia and pox virus-encoded uracil-DNA glycosylase gene eliminates viral viability [20, 25]
Summary
Vol 270, No., Issue of January 6, pp. 296-303, 1995 Printed in U.S.A. Suganthi Balasubramanian:j:§, Richard D. The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) is an acidic protein of 84 amino acids that inactivates uracil-DNA glycosylase from diverse organisms The secondary structure suggests which regions of Ugi may be involved in interactions with uracil-DNA glycosylase. Uracil residues located in the herpes simplex 1 origin of replication (Oris) hamper specific recognition by the origin binding protein [24], and inactivation of the vaccinia and pox virus-encoded uracil-DNA glycosylase gene eliminates viral viability [20, 25]. In this article we report on the determination of the secondary structure of Ugi by multidimensional nuclear magnetic resonance (NMR) utilizing isotopically labeled protein.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
