title: The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone.
abstract: Linker histone H1 plays an essential role in chromatin organization. Proper deposition of linker histone H1 as well as its removal is essential for chromatin dynamics and function. Linker histone chaperones perform this important task during chromatin assembly and other DNA-templated phenomena in the cell. Our in vitro data show that the multifunctional histone chaperone NPM1 interacts with linker histone H1 through its first acidic stretch (residues 120-132). Association of NPM1 with linker histone H1 was also observed in cells in culture. NPM1 exhibited remarkable linker histone H1 chaperone activity, as it was able to efficiently deposit histone H1 onto dinucleosomal templates. Overexpression of NPM1 reduced the histone H1 occupancy on the chromatinized template of HIV-1 LTR in TZM-bl cells, which led to enhanced Tat-mediated transactivation. These data identify NPM1 as an important member of the linker histone chaperone family in humans.
authors.affiliation: Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore, India.
authors.forename: Shrikanth S
authors.initials: SS
authors.lastname: Gadad
authors.forename: Parijat
authors.initials: P
authors.lastname: Senapati
authors.forename: Sajad Hussain
authors.initials: SH
authors.lastname: Syed
authors.forename: Roshan Elizabeth
authors.initials: RE
authors.lastname: Rajan
authors.forename: Jayasha
authors.initials: J
authors.lastname: Shandilya
authors.forename: Venkatesh
authors.initials: V
authors.lastname: Swaminathan
authors.forename: Snehajyoti
authors.initials: S
authors.lastname: Chatterjee
authors.forename: Emanuela
authors.initials: E
authors.lastname: Colombo
authors.forename: Stefan
authors.initials: S
authors.lastname: Dimitrov
authors.forename: Pier Giuseppe
authors.initials: PG
authors.lastname: Pelicci
authors.forename: Udaykumar
authors.initials: U
authors.lastname: Ranga
authors.forename: Tapas K
authors.initials: TK
authors.lastname: Kundu
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism*; D042002:Chromatin Assembly and Disassembly; D047369:Chromatin Immunoprecipitation; D057809:HEK293 Cells; D006367:HeLa Cells; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D000090243:Nucleophosmin; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid
chemical_list: D002843:Chromatin; D006657:Histones; D018832:Molecular Chaperones; C000716967:NPM1 protein, human; D009687:Nuclear Proteins; D000090243:Nucleophosmin