NAP-2: histone chaperone function and phosphorylation state through the cell cycle

Rodríguez, Pedro; Pelletier, Jerry; Price, Gerald B.; Zannis‐Hadjopoulos, Maria

doi:10.1006/jmbi.2000.3674

Cited by 63 publications

(79 citation statements)

References 42 publications

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“…NAP-2 undergoes cell-cycle-dependent changes in the phosphorylation state, and these sites are located in ␣3 and the ␣3-␣4 loop of the subdomain B. These results support the hypothesis that histone chaperone localization may be regulated by CKII-mediated phosphorylation (24). Putative phosphorylation sites in yNAP-1 were identified at positions 140, 159, and 177, all in subdomain C. Phosphorylation of these serine residues has the potential to alter the interaction of this subdomain with the NES, thus regulating NES accessibility and subcellular trafficking of NAP-1.…”

Section: Discussionsupporting

confidence: 75%

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The structure of nucleosome assembly protein 1

Park

Luger

2006

Proc. Natl. Acad. Sci. U.S.A.

193

272

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Nucleosome assembly protein 1 (NAP-1) is an integral component in the establishment, maintenance, and dynamics of eukaryotic chromatin. It shuttles histones into the nucleus, assembles nucleosomes, and promotes chromatin fluidity, thereby affecting the transcription of many genes. The 3.0 Å crystal structure of yeast NAP-1 reveals a previously uncharacterized fold with implications for histone binding and shuttling. A long ␣-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an ␣͞␤ domain is implicated in protein-protein interaction. A nuclear export sequence that is embedded in the dimerization helix is almost completely masked by an accessory domain that contains several target sites for casein kinase II. The four-stranded antiparallel ␤-sheet that characterizes the ␣͞␤ domain is found in all histone chaperones, despite the absence of homology in sequence, structural context, or quaternary structure. To our knowledge, this is the first structure of a member of the large NAP family of proteins and suggests a mechanism by which the shuttling of histones to and from the nucleus is regulated.chromatin ͉ histone chaperone ͉ nuclear transport ͉ x-ray crystallography

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Section: Discussionsupporting

confidence: 75%

“…Export of NAP depends on a nuclear export signal-like sequence (23). The mechanisms for regulating NAP-1 subcellular localization in normal cycling cells are currently unknown but may involve phosphorylationdependent regulation (24).…”

mentioning

confidence: 99%

The structure of nucleosome assembly protein 1

Park

Luger

2006

Proc. Natl. Acad. Sci. U.S.A.

193

272

View full text Add to dashboard Cite

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“…With protein B23, the binding of substrate does not affect ATP hydrolysis directly, but it appears to enhance the accessibility of the CK2 phosphorylation sites of protein B23. The stimulation of CK2 phosphorylation by substrate binding has at least one other precedent in the nucleosome assembly factors NAP-1 and NAP-2; the addition of histones enhances CK2 phosphorylation of these proteins (31). In protein B23, the increased rate of phosphorylation is dependent on the presence of the nonpolar region in the N-terminal end, since the effect is not seen when that segment is deleted.…”

Section: Figmentioning

confidence: 99%

Role of Protein Kinase CK2 Phosphorylation in the Molecular Chaperone Activity of Nucleolar Protein B23

Szebeni¹,

Hingorani²,

Negi³

et al. 2003

Journal of Biological Chemistry

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Protein B23 is a multifunctional nucleolar protein whose molecular chaperone activity is proposed to play role in ribosome assembly. Previous studies (Szebeni, A., and Olson, M. O. J. (1999) Protein Sci. 8, 905-912) showed that protein B23 has several characteristics typical of molecular chaperones, including anti-aggregation activity, promoting the renaturation of denatured proteins, and preferential binding to denatured substrates. However, until now there has been no proposed mechanism for release of a bound substrate. Protein B23 can be phosphorylated by protein kinase CK2 (CK2) in a segment required for chaperone activity. The presence of bound substrate enhanced the rate of CK2 phosphorylation of protein B23 by 2-3-fold, and this enhancement was dependent on a nonpolar region in its N-terminal end. Formation of a complex between B23 and chaperone test substrates (rhodanese or citrate synthase) was inhibited by CK2 phosphorylation. Furthermore, CK2 phosphorylation of a previously formed B23-substrate complex promoted its dissociation. The dissociation of complexes between B23 and the human immunodeficiency virus-Rev protein required both CK2 phosphorylation and competition with a Rev nuclear localization signal peptide, suggesting that Rev binds B23 at two separate sites. These studies suggest that unlike many molecular chaperones, which directly hydrolyze ATP, substrate release by protein B23 is dependent on its phosphorylation by CK2.

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“…NAP1 and NAP2 are phosphorylated in vitro by casein kinase 2. NAP2 is phosphorylated in vivo at the G o /G 1 boundary but not in S phase (47).…”

Section: Cda1 Is Phosphorylated In Vitro Bymentioning

confidence: 99%

SET-related Cell Division Autoantigen-1 (CDA1) Arrests Cell Growth

Chai

Šarčević

Mawson

et al. 2001

Journal of Biological Chemistry

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Expression of the CDA1 transgene, but not its N terminus, arrests HeLa cell growth, colony numbers, cell density, and bromodeoxyuridine uptake in a dose-dependent manner. The ability of CDA1 to arrest cell growth is abolished by mutation of the two CDK consensus phosphorylation sites. We propose that CDA1 is a negative regulator of cell growth and that its activity is regulated by its expression level and phosphorylation.

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NAP-2: histone chaperone function and phosphorylation state through the cell cycle

Cited by 63 publications

References 42 publications

The structure of nucleosome assembly protein 1

The structure of nucleosome assembly protein 1

Role of Protein Kinase CK2 Phosphorylation in the Molecular Chaperone Activity of Nucleolar Protein B23

SET-related Cell Division Autoantigen-1 (CDA1) Arrests Cell Growth

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