Asymmetry in the burial of hydrophobic residues along the histone chains of eukarya, archaea and a transcription factor.

ABSTRACT:

Background

The histone fold is a common structural motif of proteins involved in the chromatin packaging of DNA and in transcription regulation. This single chain fold is stabilized by either homo- or hetero-dimer formation in archaea and eukarya. X-ray structures at atomic resolution have shown the eukaryotic nucleosome core particle to consist of a central tetramer of two bound H3-H4 dimers flanked by two H2A-H2B dimers. The c-terminal region of the H3 histone fold involved in coupling the two eukaryotic dimers of the tetramer, through a four-fold helical bundle, had previously been shown to be a region of reduced burial of hydrophobic residues within the dimers, and thereby provide a rationale for the observed reduced stability of the H3-H4 dimer compared with that of the H2A-H2

SUBMITTER: Silverman BD 

PROVIDER: S-EPMC1283977 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature