Control of neurulation by the nucleosome assembly protein-1–like 2

10.1038/78124 ◽  
2000 ◽  
Vol 25 (4) ◽  
pp. 431-435 ◽  
Author(s):  
Ute C. Rogner ◽  
Demetri D. Spyropoulos ◽  
Nicolas Le Novère ◽  
Jean-Pierre Changeux ◽  
Philip Avner
Keyword(s):  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

Assembly states of the nucleosome assembly protein 1 (NAP-1) revealed by sedimentation velocity and non-denaturing MS

2011 ◽  
Vol 436 (1) ◽  
pp. 101-112 ◽  
Author(s):  
Masanori Noda ◽  
Susumu Uchiyama ◽  
Adam R. McKay ◽  
Akihiro Morimoto ◽  
Shigeki Misawa ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Electrostatic Interactions ◽  
Analytical Ultracentrifugation ◽  
Three Dimensional ◽  
Sedimentation Velocity ◽  
Dimensional Structure ◽  
Histone H2a ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

Proteins often exist as ensembles of interconverting states in solution which are often difficult to quantify. In the present manuscript we show that the combination of MS under nondenaturing conditions and AUC-SV (analytical ultracentrifugation sedimentation velocity) unambiguously clarifies a distribution of states and hydrodynamic shapes of assembled oligomers for the NAP-1 (nucleosome assembly protein 1). MS established the number of associated units, which was utilized as input for the numerical analysis of AUC-SV profiles. The AUC-SV analysis revealed that less than 1% of NAP-1 monomer exists at the micromolar concentration range and that the basic assembly unit consists of dimers of yeast or human NAP-1. These dimers interact non-covalently to form even-numbered higher-assembly states, such as tetramers, hexamers, octamers and decamers. MS and AUC-SV consistently showed that the formation of the higher oligomers was suppressed with increasing ionic strength, implicating electrostatic interactions in the formation of higher oligomers. The hydrodynamic shapes of the NAP-1 tetramer estimated from AUC-SV agreed with the previously proposed assembly models built using the known three-dimensional structure of yeast NAP-1. Those of the hexamer and octamer could be represented by new models shown in the present study. Additionally, MS was used to measure the stoichiometry of the interaction between the human NAP-1 dimer and the histone H2A–H2B dimer or H3–H4 tetramer. The present study illustrates a rigorous procedure for the analysis of protein assembly and protein–protein interactions in solution.

Organization and expression of the Paramecium caudatum gene encoding nucleosome assembly protein 1

Gene ◽  
2001 ◽  
Vol 280 (1-2) ◽  
pp. 107-114 ◽  
Author(s):  
Norihito Nishiyama ◽  
Shun Sawatsubashi ◽  
Masaki Ishida ◽  
Kiyoshi Yamauchi
Keyword(s):  
Paramecium Caudatum ◽  
Nucleosome Assembly ◽  
Gene Encoding ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

Self-Association of the Yeast Nucleosome Assembly Protein 1

Biochemistry ◽  
2004 ◽  
Vol 43 (32) ◽  
pp. 10592-10599 ◽  
Author(s):  
Steven J. McBryant ◽  
Olve B. Peersen
Keyword(s):  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1 ◽  
Self Association

Biochemical and Biophysical Characterisation of Higher Oligomeric Structure of Rat Nucleosome Assembly Protein 1

2017 ◽  
Vol 37 (1) ◽  
pp. 58-69
Author(s):  
Divya Reddy ◽  
Saikat Bhattacharya ◽  
Vinod Jani ◽  
Uddhavesh Sonavane ◽  
Rajendra Joshi ◽  
...  
Keyword(s):  
Nucleosome Assembly ◽  
Oligomeric Structure ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

scholarly journals Nucleosome Assembly Protein 1 Exchanges Histone H2A-H2B Dimers and Assists Nucleosome Sliding

2004 ◽  
Vol 280 (3) ◽  
pp. 1817-1825 ◽  
Author(s):  
Young-Jun Park ◽  
Jayanth V. Chodaparambil ◽  
Yunhe Bao ◽  
Steven J. McBryant ◽  
Karolin Luger
Keyword(s):  
Histone H2a ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1 ◽  
Nucleosome Sliding

scholarly journals Histone Chaperone Nap1 Is a Major Regulator of Histone H2A-H2B Dynamics at the InducibleGALLocus

2016 ◽  
Vol 36 (8) ◽  
pp. 1287-1296 ◽  
Author(s):  
Xu Chen ◽  
Sheena D'Arcy ◽  
Catherine A. Radebaugh ◽  
Daniel D. Krzizike ◽  
Holli A. Giebler ◽  
...  
Keyword(s):  
Critical Role ◽  
Histone Chaperones ◽  
Histone H2a ◽  
Nucleosome Assembly ◽  
Content Type ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1 ◽  
Histone Exchange

Histone chaperones, like nucleosome assembly protein 1 (Nap1), play a critical role in the maintenance of chromatin architecture. Here, we use theGALlocus inSaccharomyces cerevisiaeto investigate the influence of Nap1 on chromatin structure and histone dynamics during distinct transcriptional states. When theGALlocus is not expressed, cells lacking Nap1 show an accumulation of histone H2A-H2B but not histone H3-H4 at this locus. Excess H2A-H2B interacts with the linker DNA between nucleosomes, and the interaction is independent of the inherent DNA-binding affinity of H2A-H2B for these particular sequences as measuredin vitro. When theGALlocus is transcribed, excess H2A-H2B is reversed, and levels of all chromatin-bound histones are depleted in cells lacking Nap1. We developed anin vivosystem to measure histone exchange at theGALlocus and observed considerable variability in the rate of exchange across the locus in wild-type cells. We recapitulate this variability within vitronucleosome reconstitutions, which suggests a contribution of DNA sequence to histone dynamics. We also find that Nap1 is required for transcription-dependent H2A-H2B exchange. Altogether, these results indicate that Nap1 is essential for maintaining proper chromatin composition and modulating the exchange of H2A-H2Bin vivo.

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