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

Rodríguez, Pedro; Munroe, David J.; Prawitt, Dirk; Chu, Lee Lee; Bric, Eva; Kim, Jungho; Reid, Laura; Davies, Chris; Nakagama, Hitoshi; Loebbert, Ralf; Winterpacht, Andreas; Petruzzi, Mary Jane; Higgins, Michael J.; Nowak, Norma J.; Evans, Glen A.; Shows, Tom; Weissman, Bernard E.; Zabel, Bernhard; Housman, David E.; Pelletier, Jerry

doi:10.1006/geno.1997.4868

Cited by 89 publications

(87 citation statements)

References 50 publications

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“…In Drosophila, CKII phosphorylates NAP-1 (46), and there are conserved serine sites among mammalian NAPs (21). 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.…”

Section: Discussionmentioning

confidence: 99%

“…In Saccharomyces cerevisiae, a genomewide analysis showed that the expression of Ϸ10% of all genes was affected in a nap-1-deficient yeast strain. In mouse, knocking out the neuron-specific NAP-1͞2 gene resulted in embryonic lethality at the mid-gestation stage (21). Yeast NAP-1 has been shown to interact specifically with B type cyclins (clb2), kinase Gin4, and NBP (NAP-1 binding protein) (18)(19)(20).…”

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confidence: 99%

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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: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

The structure of nucleosome assembly protein 1

Park

Luger

2006

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

193

272

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“…1C). The two isoforms are most likely produced by alternative splicing, because quite similar splice variants are known for human NAP-2, a closely related protein of NAP-1, which binds linker histones as well as core histones in vitro (28). The deduced amino acid sequences also indicate that the identity between p60 xNAP-1 and human NAP-1 (hNAP-1) is as high as 88%; the identity between p60 xNAP-1 and hNAP-2 is 52%.…”

Section: Incorporation Of Linker Histones Into Dinucleosomesmentioning

confidence: 99%

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

Shintomi

Iwabuchi²,

Saeki³

et al. 2005

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

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In eukaryotic cells, genomic DNA is primarily packaged into nucleosomes through sequential ordered binding of the core and linker histone proteins. The acidic proteins termed histone chaperones are known to bind to core histones to neutralize their positive charges, thereby facilitating their proper deposition onto DNA to assemble the core of nucleosomes. For linker histones, however, little has been known about the regulatory mechanism for deposition of linker histones onto the linker DNA. Here we report that, in Xenopus eggs, the linker histone is associated with the Xenopus homologue of nucleosome assembly protein-1 (NAP-1), which is known to be a chaperone for the core histones H2A and Xenopus laevis ͉ chromatosome assembly ͉ cell-free system

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“…The protein encoded by Nap1l5 contains a region shared by members of the nucleosome assembly family of proteins. NAPs chaperone histones to the nucleus and position them onto DNA (Ito et al 1996;Rodriguez et al 1997), and are involved in transcriptional activation (Asahara et al 2002) and mitotic events (Altman and Kellogg 1997). Nap1l5 is intron-less and may have arisen through retrotransposition of another gene from the NAP family, the closest being Nap1l2.…”

Section: Figure 3 Identification and Methylation Analysis Of The Locumentioning

confidence: 99%

“…At least one other gene encoding a NAP-related protein, Nap1l4 on distal Chr 7, is regulated by genomic imprinting . It is possible that Nap1l5 does not have the same function as other NAPs, as it is truncated at the C terminus, a region thought to (Rodriguez et al 1997), and lacks a nuclear localization signal (Harada et al 2002).…”

Section: Figure 3 Identification and Methylation Analysis Of The Locumentioning

confidence: 99%

Identification of Novel Imprinted Genes in a Genome-Wide Screen for Maternal Methylation

Smith¹,

Dean²,

Konfortova³

et al. 2003

Genome Res.

166

148

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A characteristic of imprinted genes is that the maternal and paternal alleles show differences in methylation. To perform a genome-wide screen for novel imprinted loci, we applied methylation-sensitive representational difference analysis (Me-RDA) to parthenogenetic mouse embryos, to identify differentially methylated regions (DMRs) methylated specifically on the maternal allele. We isolated a total of 26 distinct clones from known and novel DMRs and identified three novel imprinted genes. Nap1l5 is located on proximal chromosome 6 and encodes a protein with homology with nucleosome assembly proteins (NAPs); it has tissue-specific imprinting with expression from the paternal allele. We identified two DMRs on chromosome 15, a chromosome that was not thought to contain imprinted loci, and demonstrated that each is associated with a paternally expressed transcript. Peg13 gives rise to a noncoding RNA that is highly expressed in the brain and imprinted in all tissues examined. A DMR was also identified at the chromosome 15 Slc38a4 gene, which encodes a system A amino acid transporter; we show that Slc38a4 is imprinted in a tissue-specific manner. Interestingly, two of the three novel genes identified in this screen are located within the introns of other genes; their identification indicates that such "microimprinted" domains may be more common than previously thought.

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

Cited by 89 publications

References 50 publications

The structure of nucleosome assembly protein 1

The structure of nucleosome assembly protein 1

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

Identification of Novel Imprinted Genes in a Genome-Wide Screen for Maternal Methylation

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