The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone

Shrikanth S. Gadad, Parijat Senapati, Sajad Hussain Syed, Roshan Elizabeth Rajan, Jayasha Shandilya, Venkatesh Swaminathan, Snehajyoti Chatterjee, Emanuela Colombo, Stefan Dimitrov, Pier Giuseppe Pelicci, Udaykumar Ranga, Tapas K. Kundu

Research output: Contribution to journalArticlepeer-review


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.(Figure Presented)

Original languageEnglish
Pages (from-to)2780-2789
Number of pages10
Issue number14
Publication statusPublished - Apr 12 2011

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone'. Together they form a unique fingerprint.

Cite this