p10, a low molecular weight single-stranded nucleic acid binding protein of murine leukemia retroviruses, shows stacking interactions of its single tryptophan residue with nucleotide bases.
Room temperature fluorescence and low-temperature phosphorescence studies of the association of p10, a basic low molecular weight single-stranded DNA binding protein isolated from murine leukemia viruses, point to the involvement of its single tryptophan residue in a close-range interaction with single-stranded polynucleotides. Optically detected triplet-state magnetic resonance (ODMR) techniques applied to the complex of p10 protein with the heavy atom derivatized polynucleotide poly(5-HgU) demonstrate the occurrence of stacking interactions of Trp35 with nucleic acid bases, thus agreeing with earlier reports that this residue is involved in the binding process [Karpel, R. L., Henderson, L. E., & Oroszlan, S. (1987) J. Biol. Chem. 262, 4961-4967].
Casas-Finet
J R
JR
Department of Chemistry, University of California, Davis 95616.
Jhon
N I
NI
Maki
A H
AH
D004268:DNA-Binding Proteins / Q000378:metabolism*; D015683:Gene Products, gag; D007700:Kinetics; D009052:Leukemia Virus, Murine / Q000378:metabolism*; D008163:Luminescent Measurements; D010084:Oxidation-Reduction; D011119:Polynucleotides / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012191:Retroviridae Proteins / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D004268:DNA-Binding Proteins; D015683:Gene Products, gag; D011119:Polynucleotides; D012191:Retroviridae Proteins; D014364:Tryptophan