scholarly journals Nucleosome Assembly Protein Gene

2020 ◽  
Author(s):  
Keyword(s):  
Protein Gene ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein

scholarly journals Tumor Suppressor NM23-H1 Is a Granzyme A-Activated DNase during CTL-Mediated Apoptosis, and the Nucleosome Assembly Protein SET Is Its Inhibitor

Cell ◽  
2003 ◽  
Vol 112 (5) ◽  
pp. 659-672 ◽  
Author(s):  
Zusen Fan ◽  
Paul J. Beresford ◽  
David Y. Oh ◽  
Dong Zhang ◽  
Judy Lieberman
Keyword(s):  
Tumor Suppressor ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Granzyme A

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 Zygotic nucleosome assembly protein–like 1 has a specific, non–cell autonomous role in hematopoiesis

Blood ◽  
2005 ◽  
Vol 106 (2) ◽  
pp. 514-520 ◽  
Author(s):  
Anita Abu-Daya ◽  
Wendy M. Steer ◽  
Alexandra F. Trollope ◽  
Christine E. Friedeberg ◽  
Roger K. Patient ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Neural Cells ◽  
Nucleosome Assembly ◽  
Globin Mrna ◽  
Blood Island ◽  
Nucleosome Assembly Protein ◽  
Hematopoietic Lineage ◽  
Core Histones ◽  
Hematopoietic Precursor ◽  
Assembly Proteins

Abstract Nucleosome assembly proteins (NAPs) bind core histones, facilitate chromatin remodeling, and can act as transcriptional coactivators. We previously described the isolation of a Xenopus NAP1-like (xNAP1L) cDNA, which encodes a member of this protein family. Its zygotic expression is restricted to neural cells, the outer cells of the ventral blood island (VBIs), and the ectoderm overlying the blood precursors. Here, we report that depletion of zygotic xNAP1L in embryos produces no obvious morphologic phenotype, but ablates α-globin mRNA expression in the VBIs. Transcript levels of the hematopoietic precursor genes SCL and Xaml (Runx-1) are also reduced in the VBIs. SCL expression can be rescued by injection of xNAP1L mRNA into the ectoderm, showing that the effect of xNAP1L can be non–cell autonomous. Fli1 and Hex, genes expressed in hemangioblasts but subsequently endothelial markers, were unaffected, suggesting that xNAP1L is required for the hematopoietic lineage specifically. Our data are consistent with a requirement for xNAP1L upstream of SCL, and injection of SCL mRNA into xNAP1L-depleted embryos rescues α-globin expression. Thus, xNAP1L, which belongs to a family of proteins previously believed to have general roles, has a specific function in hematopoiesis.

scholarly journals Combination of Hypomorphic Mutations of the Drosophila Homologues of Aryl Hydrocarbon Receptor and Nucleosome Assembly Protein Family Genes Disrupts Morphogenesis, Memory and Detoxification

PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94975 ◽  
Author(s):  
Boris A. Kuzin ◽  
Ekaterina A. Nikitina ◽  
Roman O. Cherezov ◽  
Julia E. Vorontsova ◽  
Mikhail S. Slezinger ◽  
...  
Keyword(s):  
Aryl Hydrocarbon Receptor ◽  
Protein Family ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Aryl Hydrocarbon

Assembly states of the nucleosome assembly protein 1 (NAP-1) revealed by sedimentation velocity and non-denaturing MS

2011 ◽  
Vol 436 (1) ◽  
pp. 101-112 ◽  
Author(s):  
Masanori Noda ◽  
Susumu Uchiyama ◽  
Adam R. McKay ◽  
Akihiro Morimoto ◽  
Shigeki Misawa ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Electrostatic Interactions ◽  
Analytical Ultracentrifugation ◽  
Three Dimensional ◽  
Sedimentation Velocity ◽  
Dimensional Structure ◽  
Histone H2a ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

Proteins often exist as ensembles of interconverting states in solution which are often difficult to quantify. In the present manuscript we show that the combination of MS under nondenaturing conditions and AUC-SV (analytical ultracentrifugation sedimentation velocity) unambiguously clarifies a distribution of states and hydrodynamic shapes of assembled oligomers for the NAP-1 (nucleosome assembly protein 1). MS established the number of associated units, which was utilized as input for the numerical analysis of AUC-SV profiles. The AUC-SV analysis revealed that less than 1% of NAP-1 monomer exists at the micromolar concentration range and that the basic assembly unit consists of dimers of yeast or human NAP-1. These dimers interact non-covalently to form even-numbered higher-assembly states, such as tetramers, hexamers, octamers and decamers. MS and AUC-SV consistently showed that the formation of the higher oligomers was suppressed with increasing ionic strength, implicating electrostatic interactions in the formation of higher oligomers. The hydrodynamic shapes of the NAP-1 tetramer estimated from AUC-SV agreed with the previously proposed assembly models built using the known three-dimensional structure of yeast NAP-1. Those of the hexamer and octamer could be represented by new models shown in the present study. Additionally, MS was used to measure the stoichiometry of the interaction between the human NAP-1 dimer and the histone H2A–H2B dimer or H3–H4 tetramer. The present study illustrates a rigorous procedure for the analysis of protein assembly and protein–protein interactions in solution.

scholarly journals NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B

2020 ◽  
Vol 117 (48) ◽  
pp. 30391-30399
Author(s):  
Qiang Luo ◽  
Baihui Wang ◽  
Zhen Wu ◽  
Wen Jiang ◽  
Yueyue Wang ◽  
...  
Keyword(s):  
Interaction Mechanism ◽  
Histone Chaperones ◽  
Related Protein ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Vitro Binding ◽  
Multiple Interaction ◽  
Α Helix

Nucleosome Assembly Protein 1 (NAP1) family proteins are evolutionarily conserved histone chaperones that play important roles in diverse biological processes. In this study, we determined the crystal structure ofArabidopsisNAP1-Related Protein 1 (NRP1) complexed with H2A-H2B and uncovered a previously unknown interaction mechanism in histone chaperoning. Both in vitro binding and in vivo plant rescue assays proved that interaction mediated by the N-terminal α-helix (αN) domain is essential for NRP1 function. In addition, the C-terminal acidic domain (CTAD) of NRP1 binds to H2A-H2B through a conserved mode similar to other histone chaperones. We further extended previous knowledge of the NAP1-conserved earmuff domain by mapping the amino acids of NRP1 involved in association with H2A-H2B. Finally, we showed that H2A-H2B interactions mediated by αN, earmuff, and CTAD domains are all required for the effective chaperone activity of NRP1. Collectively, our results reveal multiple interaction modes of a NAP1 family histone chaperone and shed light on how histone chaperones shield H2A-H2B from nonspecific interaction with DNA.

Organization and expression of the Paramecium caudatum gene encoding nucleosome assembly protein 1

Gene ◽  
2001 ◽  
Vol 280 (1-2) ◽  
pp. 107-114 ◽  
Author(s):  
Norihito Nishiyama ◽  
Shun Sawatsubashi ◽  
Masaki Ishida ◽  
Kiyoshi Yamauchi
Keyword(s):  
Paramecium Caudatum ◽  
Nucleosome Assembly ◽  
Gene Encoding ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

scholarly journals Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation

1994 ◽  
Vol 297 (2) ◽  
pp. 389-397 ◽  
Author(s):  
H U Simon ◽  
G B Mills ◽  
M Kozlowski ◽  
D Hogg ◽  
D Branch ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Amino Acid ◽  
Gene Product ◽  
Thymidine Incorporation ◽  
Structural Features ◽  
Nucleosome Assembly ◽  
Proliferating Cells ◽  
Amino Acid Similarity ◽  
Nucleosome Assembly Protein

We have isolated from a human thymus cDNA library a cDNA clone encoding a potential protein with 54% amino acid similarity to that encoded by a previously identified cDNA for yeast nucleosome assembly protein I (NAP-I). The deduced amino acid sequence for this newly identified cDNA, designated hNRP (human NAP-related protein), contains a potential seven-residue nuclear localization motif, three clusters of highly acidic residues and other structural features found in various proteins implicated in chromatin formation. When expressed as a fusion protein in Escherichia coli, hNRP reacted specifically with a monoclonal antibody raised against human NAP-I. The hNRP transcript was detected in all tissues and cell lines studied, but levels were somewhat increased in rapidly proliferating cells. Moreover, levels of both hNRP mRNA and protein increased rapidly in cultured T-lymphocytes induced to proliferate by incubation with phorbol ester and ionomycin. Phorbol 12-myristate 13-acetate/ionomycin-induced increases in both hNRP mRNA and mitogenesis, as measured by thymidine incorporation, were markedly inhibited, however, in cells treated with an hNRP antisense oligonucleotide. These results demonstrate a correlation between induction of hNRP expression and mitogenesis and taken together with the structural similarities between hNRP and yeast NAP-I suggest that the hNRP gene product participates in DNA replication and thereby plays an important role in the process of cell proliferation.

Self-Association of the Yeast Nucleosome Assembly Protein 1

Biochemistry ◽  
2004 ◽  
Vol 43 (32) ◽  
pp. 10592-10599 ◽  
Author(s):  
Steven J. McBryant ◽  
Olve B. Peersen
Keyword(s):  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1 ◽  
Self Association
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