L3MBTL1 recognition of mono- and dimethylated histones.
Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. An unexpected mode of peptide-mediated dimerization suggests a possible mechanism for chromatin compaction by L3MBTL1.
Min
Jinrong
J
Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario, M5G 1L5, Canada.
Allali-Hassani
Abdellah
A
Nady
Nataliya
N
Qi
Chao
C
Ouyang
Hui
H
Liu
Yongsong
Y
MacKenzie
Farrell
F
Vedadi
Masoud
M
Arrowsmith
Cheryl H
CH
D000595:Amino Acid Sequence; D002151:Calorimetry; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012097:Repressor Proteins; D017386:Sequence Homology, Amino Acid; D025521:Tumor Suppressor Proteins
D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; C120887:L3MBTL1 protein, human; D009363:Neoplasm Proteins; D012097:Repressor Proteins; D025521:Tumor Suppressor Proteins; D008239:Lysine