The ATP/ADP binding domains of actin are conserved in nucleosome complexed with histone H1 and high mobility group-17 protein.
Chromatin has been proposed to share a common evolutionary origin and analogous mechanisms of action with various structures of cytoskeleton such as actin filaments. ATP has been shown to facilitate chromatin remodelling, but the exact site of its interaction with chromatin has not been elucidated. The facts, that ATP binds specifically to actin and promotes its polymerization, led us to characterize the possible domains involved in ATP binding in nucleosome. Comparison of the sequences of actin and the protein components of nucleosome suggests that H2A may contain an adenosine binding site similar to the adenosine motif of actin, H1 and/or H2B phosphate/Ca2+ binding sites corresponding to the phosphate 1 motif of actin, HMG17 a phosphate/Ca2+ binding site corresponding to the phosphate 2 motif of actin. The ability to bind ATP may be involved in the organization of chromatin into inactive solenoid-like structures in vivo.
Tarkka
T
T
Department of Medical Biochemistry, University of Oulu, Finland.
Raatikainen
E
E
Friman
S
S
Oikarinen
J
J
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000241:Adenosine / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000737:chemistry* / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D017433:Protein Structure, Secondary; D017385:Sequence Homology
D000199:Actins; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes; D010710:Phosphates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000241:Adenosine; D002118:Calcium