Functional Characterization of Human Nucleosome Assembly Protein-2 (NAP1L4) Suggests a Role as a Histone Chaperone

Genomics ◽  
1997 ◽  
Vol 44 (3) ◽  
pp. 253-265 ◽  
Author(s):  
Pedro Rodriguez ◽  
David Munroe ◽  
Dirk Prawitt ◽  
Lee Lee Chu ◽  
Eva Bric ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Histone Chaperone ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein

Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean

1995 ◽  
Vol 249 (5) ◽  
pp. 465-473 ◽  
Author(s):  
Hae Won Yoon ◽  
Min Chul Kim ◽  
Sang Yeoul Lee ◽  
Inhwan Hwang ◽  
Jeong Dong Bahk ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Functional Characterization ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

scholarly journals OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Kangxi Du ◽  
Qiang Luo ◽  
Liufan Yin ◽  
Jiabing Wu ◽  
Yuhao Liu ◽  
...  
Keyword(s):  
Nucleosome Occupancy ◽  
Functional Characterization ◽  
Histone Chaperone ◽  
Recognition Mechanism ◽  
Developmental Defects ◽  
Dynamic Regulation ◽  
Genome Wide ◽  
Domain Protein ◽  
Acidic Region

Abstract While the yeast Chz1 acts as a specific histone-chaperone for H2A.Z, functions of CHZ-domain proteins in multicellular eukaryotes remain obscure. Here, we report on the functional characterization of OsChz1, a sole CHZ-domain protein identified in rice. OsChz1 interacts with both the canonical H2A-H2B dimer and the variant H2A.Z-H2B dimer. Within crystal structure the C-terminal region of OsChz1 binds H2A-H2B via an acidic region, pointing to a previously unknown recognition mechanism. Knockout of OsChz1 leads to multiple plant developmental defects. At genome-wide level, loss of OsChz1 causes mis-regulations of thousands of genes and broad alterations of nucleosome occupancy as well as reductions of H2A.Z-enrichment. While OsChz1 associates with chromatin regions enriched of repressive histone marks (H3K27me3 and H3K4me2), its loss does not affect the genome landscape of DNA methylation. Taken together, it is emerging that OsChz1 functions as an important H2A/H2A.Z-H2B chaperone in dynamic regulation of chromatin for higher eukaryote development.

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.

scholarly journals The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcription

Retrovirology ◽  
2008 ◽  
Vol 5 (1) ◽  
pp. 8 ◽  
Author(s):  
Chiara Vardabasso ◽  
Lara Manganaro ◽  
Marina Lusic ◽  
Alessandro Marcello ◽  
Mauro Giacca
Keyword(s):  
Histone Chaperone ◽  
Viral Transcription ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Chaperone Protein ◽  
Nucleosome Assembly Protein 1 ◽  
Hiv 1

scholarly journals Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.

1992 ◽  
Vol 12 (8) ◽  
pp. 3346-3355 ◽  
Author(s):  
M von Lindern ◽  
S van Baal ◽  
J Wiegant ◽  
A Raap ◽  
A Hagemeijer ◽  
...  
Keyword(s):  
Fusion Gene ◽  
Alternative Polyadenylation ◽  
Open Reading Frame ◽  
Sequence Motif ◽  
Nucleosome Assembly ◽  
Reading Frame ◽  
Nucleosome Assembly Protein ◽  
Gene Translocation ◽  
Translocation Breakpoints

The translocation (6;9)(p23;q34) in acute nonlymphocytic leukemia results in the formation of a highly consistent dek-can fusion gene. Translocation breakpoints invariably occur in single introns of dek and can, which were named icb-6 and icb-9, respectively. In a case of acute undifferentiated leukemia, a breakpoint was detected in icb-9 of can, whereas no breakpoint could be detected in dek. Genomic and cDNA cloning showed that instead of dek, a different gene was fused to can, which was named set. set encodes transcripts of 2.0 and 2.7 kb that result from the use of alternative polyadenylation sites. Both transcripts contain the open reading frame for a putative SET protein with a predicted molecular mass of 32 kDa. The set-can fusion gene is transcribed into a 5-kb transcript that contains a single open reading frame predicting a 155-kDa chimeric SET-CAN protein. The SET sequence shows homology with the yeast nucleosome assembly protein NAP-I. The only common sequence motif of SET and DEK proteins is an acidic region. SET has a long acidic tail, of which a large part is present in the predicted SET-CAN fusion protein. The set gene is located on chromosome 9q34, centromeric of c-abl. Since a dek-can fusion gene is present in t(6;9) acute myeloid leukemia and a set-can fusion gene was found in a case of acute undifferentiated leukemia, we assume that can may function as an oncogene activated by fusion of its 3' part to dek, set, or perhaps other genes.

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

Expression of the histone chaperone SET/TAF-Iβ during the strobilation process of Mesocestoides corti (Platyhelminthes, Cestoda)

Parasitology ◽  
2015 ◽  
Vol 142 (9) ◽  
pp. 1171-1182 ◽  
Author(s):  
CAROLINE B. COSTA ◽  
KARINA M. MONTEIRO ◽  
ALINE TEICHMANN ◽  
EDILEUZA D. DA SILVA ◽  
KARINA R. LORENZATTO ◽  
...  
Keyword(s):  
Gene Expression Regulation ◽  
Gradual Increase ◽  
Polyclonal Antibodies ◽  
Expression Patterns ◽  
Histone Chaperone ◽  
Helminth Parasites ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Partial Cdna Sequence ◽  
Partial Cdna

SUMMARYThe histone chaperone SET/TAF-Iβ is implicated in processes of chromatin remodelling and gene expression regulation. It has been associated with the control of developmental processes, but little is known about its function in helminth parasites. In Mesocestoides corti, a partial cDNA sequence related to SET/TAF-Iβ was isolated in a screening for genes differentially expressed in larvae (tetrathyridia) and adult worms. Here, the full-length coding sequence of the M. corti SET/TAF-Iβ gene was analysed and the encoded protein (McSET/TAF) was compared with orthologous sequences, showing that McSET/TAF can be regarded as a SET/TAF-Iβ family member, with a typical nucleosome-assembly protein (NAP) domain and an acidic tail. The expression patterns of the McSET/TAF gene and protein were investigated during the strobilation process by RT-qPCR, using a set of five reference genes, and by immunoblot and immunofluorescence, using monospecific polyclonal antibodies. A gradual increase in McSET/TAF transcripts and McSET/TAF protein was observed upon development induction by trypsin, demonstrating McSET/TAF differential expression during strobilation. These results provided the first evidence for the involvement of a protein from the NAP family of epigenetic effectors in the regulation of cestode development.

scholarly journals Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs

2005 ◽  
Vol 102 (23) ◽  
pp. 8210-8215 ◽  
Author(s):  
K. Shintomi ◽  
M. Iwabuchi ◽  
H. Saeki ◽  
K. Ura ◽  
T. Kishimoto ◽  
...  
Keyword(s):  
Histone Chaperone ◽  
Linker Histone ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1
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