Faculty Opinions recommendation of The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly.

2002 ◽  
Author(s):  
Song Tan
Keyword(s):  
Crystal Structure ◽  
Nucleosome Assembly ◽  
Histone Binding

scholarly journals Structure of the human histone chaperone FACT Spt16 N-terminal domain

2016 ◽  
Vol 72 (2) ◽  
pp. 121-128 ◽  
Author(s):  
G. Marcianò ◽  
D. T. Huang
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Complex Surface ◽  
Histone Chaperone ◽  
Titration Calorimetry ◽  
Nucleosome Assembly ◽  
Surface Residue ◽  
Histone Binding ◽  
Terminal Domain ◽  
Heterodimeric Complex

The histone chaperone FACT plays an important role in facilitating nucleosome assembly and disassembly during transcription. FACT is a heterodimeric complex consisting of Spt16 and SSRP1. The N-terminal domain of Spt16 resembles an inactive aminopeptidase. How this domain contributes to the histone chaperone activity of FACT remains elusive. Here, the crystal structure of the N-terminal domain (NTD) of human Spt16 is reported at a resolution of 1.84 Å. The structure adopts an aminopeptidase-like fold similar to those of theSaccharomyces cerevisiaeandSchizosaccharomyces pombeSpt16 NTDs. Isothermal titration calorimetry analyses show that human Spt16 NTD binds histones H3/H4 with low-micromolar affinity, suggesting that Spt16 NTD may contribute to histone binding in the FACT complex. Surface-residue conservation and electrostatic analysis reveal a conserved acidic patch that may be involved in histone binding.

scholarly journals Crystal Structure of Malaria Parasite Nucleosome Assembly Protein

2009 ◽  
Vol 284 (15) ◽  
pp. 10076-10087 ◽  
Author(s):  
Jasmita Gill ◽  
Manickam Yogavel ◽  
Anuj Kumar ◽  
Hassan Belrhali ◽  
S. K. Jain ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Malaria Parasite ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein

scholarly journals White spot syndrome virus protein ICP11: A histone-binding DNA mimic that disrupts nucleosome assembly

2008 ◽  
Vol 105 (52) ◽  
pp. 20758-20763 ◽  
Author(s):  
H.-C. Wang ◽  
H.-C. Wang ◽  
T.-P. Ko ◽  
Y.-M. Lee ◽  
J.-H. Leu ◽  
...  
Keyword(s):  
White Spot Syndrome Virus ◽  
White Spot ◽  
Virus Protein ◽  
Nucleosome Assembly ◽  
Histone Binding ◽  
White Spot Syndrome

scholarly journals The Cac2 subunit is essential for productive histone binding and nucleosome assembly in CAF-1

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Francesca Mattiroli ◽  
Yajie Gu ◽  
Jeremy L. Balsbaugh ◽  
Natalie G. Ahn ◽  
Karolin Luger
Keyword(s):  
Nucleosome Assembly ◽  
Histone Binding

scholarly journals The Crystal Structure of Drosophila NLP-Core Provides Insight into Pentamer Formation and Histone Binding

Structure ◽  
2003 ◽  
Vol 11 (2) ◽  
pp. 175-186 ◽  
Author(s):  
V.M.Haridasan Namboodiri ◽  
Shuchismita Dutta ◽  
Ildikó V Akey ◽  
James F Head ◽  
Christopher W Akey
Keyword(s):  
Crystal Structure ◽  
Histone Binding ◽  
Insight Into

scholarly journals Structural and histone binding studies of the chromo barrel domain of TIP60

2018 ◽  
Author(s):  
Yuzhe Zhang ◽  
Ming Lei ◽  
Xiao Liang ◽  
Peter Loppnau ◽  
Yanjun Li ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Peptide Binding ◽  
Side Chain ◽  
Titration Calorimetry ◽  
Binding Studies ◽  
Histone Tails ◽  
Histone Binding ◽  
Cellular Processes ◽  
Peptide Binding Site ◽  
Acetyltransferase Domain

AbstractTIP60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and non-histone proteins within diverse cellular processes. Whereas the TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. Here we attempted a quantitative analysis of the interaction between the TIP60-CB and histone peptides, but did not observe any binding through either fluorescence polarization or isothermal titration calorimetry. We solved a crystal structure of the TIP60-CB alone. Analysis of the crystal structure demonstrates a putative peptide binding site that may be occluded by the basic side chain of a residue in a unique β hairpin between the two N-terminal strands of the β barrel.

Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding

Biochemistry ◽  
2018 ◽  
Vol 58 (2) ◽  
pp. 108-113 ◽  
Author(s):  
Prithwijit Sarkar ◽  
Naifu Zhang ◽  
Sudipta Bhattacharyya ◽  
Karlah Salvador ◽  
Sheena D’Arcy
Keyword(s):  
Caenorhabditis Elegans ◽  
Nucleosome Assembly ◽  
Histone Binding ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1
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