The number of PML nuclear bodies increases in early S phase by a fission mechanism.
Promyelocytic leukemia (PML) nuclear bodies have been implicated in a variety of cellular processes including apoptosis, tumour suppression, anti-viral response, DNA repair and transcriptional regulation. PML nuclear bodies are both positionally and structurally stable over extended periods of interphase. As demonstrated in this study, the structural stability is lost as cells enter S phase, evidenced both by distortions in shape and by fission and fusion events. At the end of this period of structural instability, the number of PML nuclear bodies has increased by a factor of twofold. Association of the fission products with chromatin implies that the PML nuclear bodies respond to changes in chromatin organisation or topology, and thus could play a role in monitoring genome integrity during DNA synthesis or in the continued maintenance of functional chromosomal domains prior to mitosis.
Programme in Cell Biology, The Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, M5G 1X8 Canada.
Graham
G
Dellaire
Reagan W
RW
Ching
Hesam
H
Dehghani
Ying
Y
Ren
David P
DP
Bazett-Jones
D045744:Cell Line, Tumor; D002843:Chromatin / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D045586:Intranuclear Inclusion Bodies / Q000378:metabolism / Q000648:ultrastructure*; D009363:Neoplasm Proteins / Q000378:metabolism / Q000648:ultrastructure*; D015530:Nuclear Matrix / Q000378:metabolism / Q000648:ultrastructure; D009687:Nuclear Proteins / Q000378:metabolism / Q000648:ultrastructure*; D000071156:Promyelocytic Leukemia Protein; D016196:S Phase / Q000502:physiology*; D014157:Transcription Factors / Q000378:metabolism / Q000648:ultrastructure*; D025521:Tumor Suppressor Proteins / Q000378:metabolism / Q000648:ultrastructure*
D002843:Chromatin; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D000071156:Promyelocytic Leukemia Protein; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; C070576:PML protein, human