Summary information and primary citation
- PDB-id
-
7u47;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- cryo-EM (7.5 Å)
- Summary
- Cryoem structure of cenp-n promoted nucleosome stacks
with cenp-a and palindromic alpha satellite DNA
sequence
- Reference
-
Zhou K, Gebala M, Woods D, Sundararajan K, Edwards G,
Krzizike D, Wereszczynski J, Straight AF, Luger K (2022):
"CENP-N
promotes the compaction of centromeric chromatin."
Nat.Struct.Mol.Biol., 29,
403-413. doi: 10.1038/s41594-022-00758-y.
- Abstract
- The histone variant CENP-A is the epigenetic
determinant for the centromere, where it is interspersed
with canonical H3 to form a specialized chromatin structure
that nucleates the kinetochore. How nucleosomes at the
centromere arrange into higher order structures is unknown.
Here we demonstrate that the human CENP-A-interacting
protein CENP-N promotes the stacking of CENP-A-containing
mononucleosomes and nucleosomal arrays through a previously
undefined interaction between the α6 helix of CENP-N with
the DNA of a neighboring nucleosome. We describe the
cryo-EM structures and biophysical characterization of such
CENP-N-mediated nucleosome stacks and nucleosomal arrays
and demonstrate that this interaction is responsible for
the formation of densely packed chromatin at the centromere
in the cell. Our results provide first evidence that
CENP-A, together with CENP-N, promotes specific chromatin
higher order structure at the centromere.
