Nucleoside triphosphate binding and hydrolysis by histone H1.
We present here further evidence supporting that histone H1 contains a nucleotide binding site interacting e.g. with ADP, ATP, GDP and GTP. The finding is in accordance with the previous observation that nucleotides modulate recognition of DNA by H1. Most interestingly, H1 appears to be capable of hydrolyzing NTPs and incorporating phosphate to exogenous proteins. The mode of nucleotide action on H1 may be considered highly analogous to that of GTPases. Nuclear receptors may thus act through mechanisms similar to those for receptors on the plasma membrane.
Mannermaa
R M
RM
Collagen Research Unit, University of Oulu, Finland.
Oikarinen
J
J
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002846:Chromatography, Affinity; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D008099:Liver / Q000378:metabolism; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding; D051381:Rats; D012265:Ribonucleotides / Q000378:metabolism*
D004268:DNA-Binding Proteins; D006657:Histones; D009707:Nucleosomes; D012265:Ribonucleotides; D000105:Acetyl Coenzyme A; D000255:Adenosine Triphosphate; D004247:DNA