Structure and function of nucleosome assembly proteins.
Homologues of nucleosome assembly protein 1 (NAP1) have been identified in all eukaryotes. Although initially identified as histone chaperones and chromatin-assembly factors, additional functions include roles in tissue-specific transcription regulation, apoptosis, histone shuttling, and cell-cycle regulation, and extend beyond those of a simple chaperone and assembly factor. NAP1 family members share a structurally conserved fold, the NAP domain. Here we review current knowledge of the NAP family of proteins within the context of the recently determined crystal structure of the NAP1 family's first representative, NAP1 from yeast.
Park
Young-Jun
YJ
Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biology, CO State University, Fort Collins, CO 80523-1870, USA. yjpark@lamar.colostate.edu
Luger
Karolin
K
D021581:Active Transport, Cell Nucleus; D000818:Animals; D017209:Apoptosis; D002453:Cell Cycle; D018797:Cell Cycle Proteins / Q000235:genetics* / Q000502:physiology*; D042002:Chromatin Assembly and Disassembly; D006801:Humans; D008297:Male; D008954:Models, Biological; D018832:Molecular Chaperones / Q000235:genetics / Q000502:physiology; D005810:Multigene Family; D009687:Nuclear Proteins / Q000235:genetics* / Q000502:physiology*; D056490:Nucleosome Assembly Protein 1; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D014158:Transcription, Genetic
D018797:Cell Cycle Proteins; D018832:Molecular Chaperones; C533557:NAP1L1 protein, human; D009687:Nuclear Proteins; D056490:Nucleosome Assembly Protein 1