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© The Rockefeller University Press, 0021-9525/1999//221 $5.00
The Journal of Cell Biology, Volume 147, Number 2, , 1999 221-234

Original Article

Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1



Alexander M. Ishova, Alexey G. Sotnikova, Dmitri Negoreva, Olga V. Vladimirovaa, Norma Neffb, Tetsu Kamitanic, Edward T.H. Yehc, Jerome F. Strauss, IIId, and Gerd G. Maula

a The Wistar Institute, Philadelphia, Pennsylvania 19104
b Kimball Research Institute, New York, New York 10021
c Division of Molecular Medicine, University of Texas Health Center, Houston, Texas 77030
d Department of Obstetrics and Gynecology, University of Pennsylvania, Philadelphia, Pennsylvania 19104
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104.(215) 898-3868(215) 898-3817

maul{at}wista.wistar.upenn.edu

Nuclear domain 10 (ND10), also referred to as nuclear bodies, are discrete interchromosomal accumulations of several proteins including promyelocytic leukemia protein (PML) and Sp100. In this study, we investigated the mechanism of ND10 assembly by identifying proteins that are essential for this process using cells lines that lack individual ND10-associated proteins. We identified the adapter protein Daxx and BML, the RecQ helicase missing in Bloom syndrome, as new ND10-associated proteins. PML, but not BLM or Sp100, was found to be responsible for the proper localization of all other ND10-associated proteins since they are dispersed in PML–/– cells. Introducing PML into this cell line by transient expression or fusion with PML-producing cells recruited ND10-associated proteins into de novo formed ND10 attesting to PMLs essential nature in ND10 formation. In the absence of PML, Daxx is highly enriched in condensed chromatin. Its recruitment to ND10 from condensed chromatin requires a small ubiquitin-related modifier (SUMO-1) modification of PML and reflects the interaction between the COOH-terminal domain of Daxx and PML. The segregation of Daxx from condensed chromatin in the absence of PML to ND10 by increased accumulation of SUMO-1–modified PML suggests the presence of a variable equilibrium between these two nuclear sites. Our findings identify the basic requirements for ND10 formation and suggest a dynamic mechanism for protein recruitment to these nuclear domains controlled by the SUMO-1 modification state of PML.

Key Words: nuclear structure • nuclear proteins • protein interaction • supramolecular regulation • knockout cells

© 1999 The Rockefeller University Press

1.used in this paper: APC, acute promyelocytic leukemia; BSF, human Bloom syndrome–derived primary fibroblasts; Daxx, Fas death domain–associated protein; HF, human primary fibroblasts; MPEF, embryonic primary mouse fibroblasts; ND10, nuclear domain 10; NGP, human neuroblastoma cells; PML, promyelocytic leukemia protein; PML–/– MPEF, SV40 large T-antigen transformed cells derived from embryos of PML–/– knockout mouse; Sp100, autoantigen in primary billiary cirrhosis; SUMO-1, small ubiquitin-related modifier


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