Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity.

Fujii-Nakata, Tomoko; Ishimi, Yukio; Okuda, Asuko; Kikuchi, Atsumi

doi:10.1016/s0021-9258(19)36785-7

Cited by 144 publications

(24 citation statements)

References 29 publications

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“…We next tested whether the N terminus of CAL1 can mediate CENP-A assembly in vitro using a plasmid supercoiling assay (Fujii-Nakata et al, 1992;Clark and Leblanc, 2009) and three different N-terminal truncations (1-96, 1-132, and 1-160; Fig. S5 D) CAL1 form a complex with CENP-A and histone H4 when the three proteins are co-expressed (Fig.…”

Section: Cal1 1-160 Displays Cenp-a Nucleosome Assembly Activity In Vitromentioning

confidence: 99%

CAL1 is the Drosophila CENP-A assembly factor

Chen

Dechassa

Bettini

et al. 2014

Journal of Cell Biology

133

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Section: Cal1 1-160 Displays Cenp-a Nucleosome Assembly Activity In Vitromentioning

confidence: 99%

CAL1 is the Drosophila CENP-A assembly factor

Chen

Dechassa

Bettini

et al. 2014

Journal of Cell Biology

133

159

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“…The purified protein was given the name NAP1 (nucleosome assembly protein 1), and a monoclonal antibody raised against it was found to recognize a protein of similar molecular weight in Drosophila and yeast (Ishimi et al, 1985). This antibody was used to clone the S. cerevisiae homolog of NAP1, which was also found to promote nucleosome assembly in vitro (Fujii-Nakata et al, 1992;Ishimi and Kikuchi, 1991). The relevance of NAPI's ability to drive nucleosome assembly in vitro to its in vivo function is unclear.…”

Section: The In Vivo Function Of Nap1mentioning

confidence: 99%

Members of the NAP/SET family of proteins interact specifically with B-type cyclins.

Kellogg

Kikuchi

Fujii-Nakata

et al. 1995

The Journal of Cell Biology

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Abstract. Cyclin-dependent kinase complexes that contain the same catalytic subunit are able to induce different events at different times during the cell cycle, but the mechanisms by which they do so remain largely unknown. To address this problem, we have used affinity chromatography to identify proteins that bind specifically to mitotic cyclins, with the goal of finding proteins that interact with mitotic cyclins to carry out the events of mitosis. This approach has led to the identification of a 60-kD protein called NAP1 that interacts specifically with members of the cyclin B family. This interaction has been highly conserved during evolution: NAP1 in the Xenopus embryo interacts with cyclins B1 and B2, but not with cyclin A, and the S. cerevisiae homolog of NAP1 interacts with Clb2 but not with Clb3.Genetic experiments in budding yeast indicate that NAP1 plays an important role in the function of Clb2, while biochemical experiments demonstrate that purified NAP1 can be phosphorylated by cyclin B/p34 ~c2 kinase complexes, but not by cyclin A/p34 cd~2 kinase complexes. These results suggest that NAP1 is a protein involved in the specific functions of cyclin B/p34 cdc2 kinase complexes. In addition to NAP1, we found a 43-kD protein in Xenopus that is homologous to NAP1 and also interacts specifically with B-type cyclins. This protein is the Xenopus homolog of the human SET protein, which was previously identified as part of a putative oncogenic fusion protein (Von Lindern et al., 1992). pASSAgE through the eukaryotic cell cycle is controlled by the activity of protein kinase complexes that are composed of an activating subunit (a cyclin) and a catalytic subunit (a cyclin-dependent kinase [Cdk]l; for reviews see Murray and Hunt, 1993;Norbury and Nurse, 1992). Cyclins were originally identified as proteins that fluctuate in abundance during the cell cycle (Evans et al., 1983), while cyclin-dependent kinases were identified genetically as the products of genes required for cell cycle progression in yeasts (the CDC28 gene in S. cerevisiae and the homologous cdc2 gene in S. pombe) (Hartwell et al., 1974;Nurse and Thuriaux, 1980). An active cyclin-dependent kinase complex was first identified biochemically as purified maturation promoting factor (MPF), an activity from Xenopus eggs that can drive cells into mitosis and meiosis (Dunphy et al., 1988;Gautier et al., 1988;Lohka et al., 1988 As of August 1995, the address of D. R. Kellogg will be the Department of Biology, Sinsheimer Laboratories, University of California, Santa Cruz, CA 95064. Abbreviations used in this paper:Cdk, cyclin-dependent kinase; GST, glutathione-S-transferase; LB, Luria-Beltrani media; NAP1, nucleosome assembly protein 1.The cell cycle of the budding yeast S. cerevisiae is driven by a single cyclin-dependent kinase called p34 Cotes, which is activated during G1 by association with members of the G1 class of cyclins (encoded by three CLN genes), and during S phase and mitosis by association with the B-type cyclins (encoded by 6 CLB genes) (Ep...

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“…Higher order packing of nucleosomes is However, the situation is clearly more complex as CAF1 controlled by histone chaperones and remodeling mamediates nucleosome assembly in the vicinity of replicachines that may participate in transcriptional regulation tion forks (Smith and Stillman, 1989). (Razin, 1998; Pazin and Kadonaga, 1997;Kadonaga, In general, little is known about chaperone-histone inter-1998). For example, histone acetyl transferases regulate actions, although charge complimentarity is thought to be important.…”

Section: Introductionmentioning

confidence: 99%

“…In this work, it was suggested that Np may domain would be a good candidate for crystallization replace sperm basic proteins, termed X and Y, with H2A/ (Figure 1B). In addition, circular dichroism indicated that H2B dimers to generate nucleosomes (Leno et al, 1996; ‫%05ف‬ of the residues within Np may adopt a random coil Philpott and Leno, 1992) (see Table 1). Nucleoplasmin is a prominent substrate for develop-We find that the Np-core monomer forms an eightmentally regulated phosphorylation.…”

Section: Introductionmentioning

confidence: 99%

The Crystal Structure of Nucleoplasmin-Core

et al. 2001

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The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 A resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. In the crystal, two pentamers associate to form a decamer. We show that both Np and Np-core are competent to assemble large complexes that contain the four core histones. Further experiments and modeling suggest that these complexes each contain five histone octamers which dock to a central Np decamer. This work has important ramifications for models of histone storage, sperm chromatin decondensation, and nucleosome assembly.

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Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity.

Cited by 144 publications

References 29 publications

CAL1 is the Drosophila CENP-A assembly factor

CAL1 is the Drosophila CENP-A assembly factor

Members of the NAP/SET family of proteins interact specifically with B-type cyclins.

The Crystal Structure of Nucleoplasmin-Core

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