Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0003-9861(02)00721-X
Title: Rice HMGB1 protein recognizes DNA structures and bends DNA efficiently
Authors: Wu, Q. 
Zhang, W.
Pwee, K.-H. 
Kumar, P.P. 
Keywords: Circular dichroism
DNA bending
DNA binding
Electrophoretic mobility shift assay
Recombinant HMGB1
Rice HMGB1 protein
Issue Date: 1-Mar-2003
Source: Wu, Q., Zhang, W., Pwee, K.-H., Kumar, P.P. (2003-03-01). Rice HMGB1 protein recognizes DNA structures and bends DNA efficiently. Archives of Biochemistry and Biophysics 411 (1) : 105-111. ScholarBank@NUS Repository. https://doi.org/10.1016/S0003-9861(02)00721-X
Abstract: We analyzed the DNA-binding and DNA-bending properties of recombinant HMGB1 proteins based on a rice HMGB1 cDNA. Electrophoretic mobility shift assay demonstrated that rice HMGB1 can bind synthetic four-way junction (4H) DNA and DNA minicircles efficiently but the binding to 4H can be completed out by HMGA and histone H1. Conformational changes were detected by circular dichroism analysis with 4H DNA bound to various concentrations of HMGB1 or its truncated forms. T4 ligase-mediated circularization assays with short DNA fragments of 123 bp showed that the protein is capable of increasing DNA flexibility. The 123-bp DNA formed closed circular monomers efficiently in its presence, similar to that in an earlier study on maize HMG. Additionally, our results show for the first time that the basic N-terminal domain enhances the affinity of the plant HMGB1 protein for 4H DNA, while the acidic C-terminal domain has the converse effects. © 2003 Elsevier Science (USA). All rights reserved.
Source Title: Archives of Biochemistry and Biophysics
URI: http://scholarbank.nus.edu.sg/handle/10635/101602
ISSN: 00039861
DOI: 10.1016/S0003-9861(02)00721-X
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