Nonsequence-specific arginine interactions in the nucleosome core particle
Nonsequence-specific arginine interactions in the nucleosome core particle
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DOI:
10.1002/bip.10389
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发表时间:
2003-08-01
期刊:
影响因子:
2.9
通讯作者:
Subirana, JA
中科院分区:
文献类型:
--
作者:
García-Pérez, M;Pinto, M;Subirana, JA
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. (C) 2003 Wiley Periodicals, Inc.