Nonsequence-specific arginine interactions in the nucleosome core particle.
We have analyzed the relative orientation of basic amino acid side chains towards DNA in the nucleosome core particle. The electric field created by DNA phosphates has no apparent preferential orientation: no favored orientation of the arginine guanidinium group is found. Arginine may be either directly hydrogen bonded to a phosphate oxygen or stabilized in the minor groove by van der Waals contacts and the local negative electric field. On the other hand, the phosphate oxygen atoms hydrogen bonded to arginines are always found close to the plane defined by the guanidinium group. Thus it can be concluded that the interactions of arginine are strongly directional, those of phosphate are not. We also find that a highly charged fragment of histone H2B, which is placed between two DNA turns, has a very variable conformation. An increase in protein positive charge density apparently allows multiple nonspecific protein conformations when interacting with DNA.
García-Pérez
Maria
M
Departament d'Enginyeria Química, E. T. S. Enginyeria Industrial de Barcelona, Universitat Politécnica de Catalunya, Av. Diagonal 647, E08028 Barcelona, Spain.
Pinto
Marta
M
Subirana
Juan A
JA
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000737:chemistry*; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry; D006657:Histones / Q000737:chemistry*; D006801:Humans; D009707:Nucleosomes / Q000737:chemistry*; D011485:Protein Binding
D004268:DNA-Binding Proteins; D006657:Histones; D009707:Nucleosomes; D001120:Arginine