Asset Details
Do you wish to reserve the book?
Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
Do you wish to request the book?
Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
2002
Overview
Specific modifications to histones are essential epigenetic markers
1
—heritable changes in gene expression that do not affect the DNA sequence. Methylation of lysine 9 in histone H3 is recognized by heterochromatin protein 1 (HP1), which directs the binding of other proteins to control chromatin structure and gene expression
2
,
3
,
4
. Here we show that HP1 uses an induced-fit mechanism for recognition of this modification, as revealed by the structure of its chromodomain bound to a histone H3 peptide dimethylated at N
ζ
of lysine 9. The binding pocket for the
N
-methyl groups is provided by three aromatic side chains, Tyr 21, Trp 42 and Phe 45, which reside in two regions that become ordered on binding of the peptide. The side chain of Lys 9 is almost fully extended and surrounded by residues that are conserved in many other chromodomains. The QTAR peptide sequence preceding Lys 9 makes most of the additional interactions with the chromodomain, with HP1 residues Val 23, Leu 40, Trp 42, Leu 58 and Cys 60 appearing to be a major determinant of specificity by binding the key buried Ala 7. These findings predict which other chromodomains will bind methylated proteins and suggest a motif that they recognize.
Publisher
Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
Subject
/ Animals
/ Biological and medical sciences
/ Chromosomal Proteins, Non-Histone - chemistry
/ Chromosomal Proteins, Non-Histone - metabolism
/ DNA
/ Fundamental and applied biological sciences. Psychology
/ Genes
/ Humanities and Social Sciences
/ letter
/ lysine
/ Magnetic Resonance Spectroscopy
/ Mice
/ Molecular and cellular biology
/ Peptides
/ Proteins
/ Recombinant Fusion Proteins - chemistry
/ Science
