N
Natalia V. Murzina
Researcher at University of Cambridge
Publications - 13
Citations - 2245
Natalia V. Murzina is an academic researcher from University of Cambridge. The author has contributed to research in topics: Histone code & Histone H3. The author has an hindex of 12, co-authored 13 publications receiving 2135 citations.
Papers
More filters
Journal ArticleDOI
Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9.
Peter R. Nielsen,Daniel Nietlispach,Helen R. Mott,Juliana Callaghan,Andrew J. Bannister,Tony Kouzarides,Alexey G. Murzin,Natalia V. Murzina,Ernest D. Laue +8 more
TL;DR: It is shown that HP1 uses an induced-fit mechanism for recognition of methylation of lysine 9 in histone H3, which predicts which other chromodomains will bind methylated proteins and suggest a motif that they recognize.
Journal ArticleDOI
The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer
Sally V. Brasher,Brian O. Smith,Rasmus H. Fogh,Daniel Nietlispach,Abarna Thiru,Peter R. Nielsen,R. William Broadhurst,Linda J. Ball,Natalia V. Murzina,Ernest D. Laue +9 more
TL;DR: Results suggest that chromo domains may function as protein interaction motifs, bringing together different proteins in multi‐protein complexes and locating them in heterochromatin.
Journal ArticleDOI
Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins.
TL;DR: It is suggested that CAF-1 p150 has a heterochromatin-specific function distinct from its nucleosome assembly function during S phase, as histone H3 is dephosphorylated just before mitosis.
Journal ArticleDOI
Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin.
Abarna Thiru,Daniel Nietlispach,Helen R. Mott,Mitsuru Okuwaki,Debbie Lyon,Peter R. Nielsen,Miriam Hirshberg,Alain Verreault,Natalia V. Murzina,Ernest D. Laue +9 more
TL;DR: It is shown that targeting of HP1β to heterochromatin requires shadow domain interactions with PXVXL‐containing proteins in addition to chromo domain recognition of Lys‐9‐methylated histone H3, and this finding implies a further complexity to the histone code for regulation of chromatin structure and suggests how binding ofHP1 family proteins may lead to its condensation.
Journal ArticleDOI
Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46
Natalia V. Murzina,Xue-Yuan Pei,Wei Zhang,Mike Sparkes,Jose Vicente-Garcia,J. Venkatesh Pratap,Stephen H. McLaughlin,Tom Rolef Ben-Shahar,Alain Verreault,Ben F. Luisi,Ernest D. Laue +10 more
TL;DR: The crystal structure of human RbAp46 bound to histone H4 is reported, suggesting that when a hist one H3/H4 dimer (or tetramer) binds to R bAp46 or Rb Ap48, helix 1 of histoneH4 unfolds to interact with the histone chaperone.