NDLI: DNA binding ability of histone-like protein HPhA is negatively affected by interaction with Pb2+

Content Provider	Springer Nature Link
Author	Wang, Yanyan Wang, Ye Zhan, Yang Zhang, Jinrui Liang, Weiguo Fang, Xuexun Yu, Dahai Feng, Yan
Copyright Year	2015
Abstract	The histone-like protein (HPhA) is highly homologous to the eukaryotic histones and has the ability to bind to the DNA molecules. In this study, we tested divalent metal ions Mg2+, Ca2+, Zn2+, Pb2+ for their effect on the recombinant HPhA (rHPhA)-DNA binding. We found that only Pb2+ was able to reduce the formation of rHPhA-DNA complex using gel mobility shift assays. Equilibrium dialysis showed that Pb2+ bound to rHPhA by a 2:1 ratio. The interaction of Pb2+ and rHPhA was further studied by spectroscopic method including fluorescence, ultraviolet visible (UV–Vis) absorption, and circular dichroism (CD) spectroscopies. Fluorescent spectroscopy results suggested that Pb2+ and rHPhA formed a complex that caused internal quenching of the fluorescence of the protein at the ground state, and the quenching is predominately static and mixed with dynamic quenching. UV–Vis absorption spectrum results showed Pb2+ caused a slightly blue shift of the maximum absorption wavelength of rHPhA which indicated the reduction of the protein’s hydrophobicity. The CD spectrum further indicated that a reduction of the α-helix content of rHPhA occurred upon binding to Pb2+. Synchronous fluorescence spectrometry analysis revealed that Pb2+ was able to affect the polarity of the amino acids that near the Trp and Tyr residues. These results together showed that Pb2+ interact with the recombinant rHPhA and this interaction negatively affect the ability of rHPhA to form complex with DNA molecules.
Starting Page	207
Ending Page	217
Page Count	11
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	28
Issue Number	1
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2015-01-08
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Histone-like protein Protein-DNA complex Pb2+ Metal-binding proteins Metal-protein interaction Biochemistry Pharmacology/Toxicology Microbiology Cell Biology Plant Physiology Medicine/Public Health
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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