A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B

Mosammaparast, Nima; Ewart, Courtney S.; Pemberton, Lucy F.

doi:10.1093/emboj/cdf647

Cited by 171 publications

(268 citation statements)

References 44 publications

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“…Oligomerization of various Nap1 orthologs occurs in vivo and under physiological conditions in vitro (Ishimi et al , 1983, 1984; Fujii‐Nakata et al , 1992; Chang et al , 1997; Mosammaparast et al , 2002; McBryant & Peersen, 2004; Toth et al , 2005; Park et al , 2008; Noda et al , 2011; Newman et al , 2012). The biological role of Nap1 oligomerization has so far remained unclear.…”

Section: Resultsmentioning

confidence: 99%

“…Depending on the method of analysis, the ionic strength, and concentration used, different oligomerization states of Nap1 dimers have been reported. In size‐exclusion chromatography, purified yNap1 alone or in complex with H2A–H2B elutes as a broad peak indicative of a heterogeneous mixtures of various oligomeric species (Mosammaparast et al , 2002; Park et al , 2008). The crystal structure of yNap1c in the absence of histones revealed an extended β5–β6 hairpin that is involved in crystal packing (Park et al , 2008).…”

Section: Resultsmentioning

confidence: 99%

“…One possibility is that oligomerization plays a role in such nucleocytoplasmic shuttling. A nuclear export sequence (NES) has been identified and experimentally confirmed in residues 88–102 (Mosammaparast et al , 2002; Miyaji‐Yamaguchi et al , 2003). Due to continuous NES‐dependent export from the nucleus, the majority of yNAP1 is present in the cytoplasm (Mosammaparast et al , 2002; Miyaji‐Yamaguchi et al , 2003).…”

Section: Discussionmentioning

confidence: 99%

“…As one copy of H2A–H2B organizes about ~30 bp of nucleosomal DNA (Luger et al , 1997), it is likely that these smaller nucleosomes correspond to hexasomes, assembly intermediates lacking one copy of H2A–H2B. yNap1 is involved in nuclear transport of H2A–H2B (Mosammaparast et al , 2002), but we exclude the possibility that the nucleosome assembly defect we observe in the nap1 Δ strain is due to lack of nuclear H2A–H2B. Nap1 deletion only modestly reduces the amounts of nuclear H2A–H2B indicating that there are redundant H2A–H2B transport mechanisms (Mosammaparast et al , 2001).…”

Section: Discussionmentioning

confidence: 99%

“…Due to continuous NES‐dependent export from the nucleus, the majority of yNAP1 is present in the cytoplasm (Mosammaparast et al , 2002; Miyaji‐Yamaguchi et al , 2003). The karyopherin Kap114p binds a region of yNap1 that contains putative nuclear localization sequence (NLS) in residues 290–295 (Mosammaparast et al , 2002; Miyaji‐Yamaguchi et al , 2003). The region comprising this putative NLS has been implicated in oligomerization of isolated yNap1 presumably resulting in a form that is inhibitory for nuclear transport as burial of the NLS is predicted to prevent interaction with Kap114p (Park et al , 2008).…”

Section: Discussionmentioning

confidence: 99%

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Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

et al. 2016

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Nap1 is a histone chaperone involved in the nuclear import of H2A–H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A–H2B together with in vitro and in vivo functional studies that elucidate the principles underlying Nap1‐mediated H2A–H2B chaperoning and nucleosome assembly. A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A–H2B heterodimer. Oligomerization of the Nap1–H2A–H2B complex results in burial of surfaces required for deposition of H2A–H2B into nucleosomes. Chromatin immunoprecipitation‐exonuclease (ChIP‐exo) analysis shows that Nap1 is required for H2A–H2B deposition across the genome. Mutants that interfere with Nap1 oligomerization exhibit severe nucleosome assembly defects showing that oligomerization is essential for the chaperone function. These findings establish the molecular basis for Nap1‐mediated H2A–H2B deposition and nucleosome assembly.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

et al. 2016

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Sudden infant death with dysgenesis of the testes syndrome in a non‐Amish infant: A case report

Slater

Glinton

Dai

et al. 2020

American J of Med Genetics Pt A

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Sudden Infant Death with Dysgenesis of the Testes syndrome (SIDDT) is a very rare condition associated with biallelic pathogenic variants in the TSPYL1 gene first reported in 2004. It is characterized by sudden cardiac or respiratory arrest, disordered testicular development, neurologic dysfunction, and is uniformly fatal before the age of 12 months. There were previously 21 reported cases of SIDDT in the literature, all from nine Old Order Amish families published in a single paper. In this report, we describe a non-Amish, phenotypically female infant with poor feeding and abnormal motor movements noted at birth. Initial testing showed that she had a 46,XY chromosome complement, and chromosomal microarray showed a significant absence of heterozygosity (AOH) totalling roughly 600 Mb across multiple different chromosomes, indicating consanguinity. Further workup with exome sequencing revealed homozygosity for a frameshift variant in TSPYL1 (c.725_726delTG, p.Val242GlufsTer52) consistent with a diagnosis of SIDDT, explaining many of her clinical features. However, she was also noted to have a mild T-cell lymphopenia and developed intractable epilepsy after hospital discharge. These features have not previously been reported in SIDDT and may represent phenotypic expansion. To our knowledge, this patient is the 22nd case of SIDDT to be reported in the literature, and the first to be of non-Amish heritage.

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Septin‐associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae

Perez

Thorner

2018

Cytoskeleton

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In budding yeast, a collar of septin filaments at the neck between a mother cell and its bud marks the incipient site for cell division and serves as a scaffold that recruits proteins required for proper spatial and temporal execution of cytokinesis. A set of interacting proteins that localize at or near the bud neck, including Aim44/Gps1, Nba1 and Nis1, also has been implicated in preventing Cdc42‐dependent bud site re‐establishment at the division site. We found that, at their endogenous level, Aim44 and Nis1 robustly localize sequentially at the septin collar. Strikingly, however, when overproduced, both proteins shift their subcellular distribution predominantly to the nucleus. Aim44 localizes with the inner nuclear envelope, as well as at the plasma membrane, whereas Nis1 accumulates within the nucleus, indicating that these proteins normally undergo nucleocytoplasmic shuttling. Of the 14 yeast karyopherins, Kap123/Yrb4 is the primary importin for Aim44, whereas several importins mediate Nis1 nuclear entry. Conversely, Kap124/Xpo1/Crm1 is the primary exportin for Nis1, whereas both Xpo1 and Cse1/Kap109 likely contribute to Aim44 nuclear export. Even when endogenously expressed, Nis1 accumulates in the nucleus when Nba1 is absent. When either Aim44 or Nis1 are overexpressed, Nba1 is displaced from the bud neck, further consistent with the mutual interactions of these proteins. Collectively, our results indicate that a previously unappreciated level at which localization of septin‐associated proteins is controlled is via regulation of their nucleocytoplasmic shuttling, which places constraints on their availability for complex formation with other partners at the bud neck.

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A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B

Cited by 171 publications

References 44 publications

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

Sudden infant death with dysgenesis of the testes syndrome in a non‐Amish infant: A case report

Septin‐associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae

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