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First published online 18 January 2005
doi: 10.1242/jcs.01605

Journal of Cell Science 118, 611-622 (2005)
Published by The Company of Biologists 2005
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Research Article

Satellite DNA binding and cellular localisation of RNA helicase P68

Natella Enukashvily1,*, Rossen Donev2,{ddagger}, Denise Sheer2 and Olga Podgornaya1

1 Cell Cultures Department, Institute of Cytology, Tikhoretsky, 4, St Petersburg, 194064, Russia
2 Human Cytogenetics Laboratory, Cancer Research UK London Research Institute, Lincoln's Inn Fields, London WC2A 3PX, UK

* Author for correspondence (e-mail: natella{at}mail.ctyspb.rssi.ru)

Accepted 25 October 2004

We purified a 68-kDa protein from the mouse nuclear matrix using ion exchange and affinity chromatography. Column fractions were tested for specific binding to mouse minor satellite DNA using a gel mobility shift assay. The protein was identified by mass spectrometry as RNA helicase P68. In fixed cells, P68 was found to shuttle in and out of SC35 domains, forming fibres and granules in a cell-cycle dependent manner. Analysis of the P68 sequence revealed a short potential coiled-coil domain that might be involved in the formation of P68 fibres. Contacts between centromeres and P68 granules were observed during all phases of the cycle but they were most prominent in mitosis. At this stage, P68 was found in both the centromeric regions and the connections between chromosomes. Direct interaction of P68/DEAD box RNA helicase with satellite DNAs in vitro has not been demonstrated for any other members of the RNA helicase family.

Key words: RNA helicase P68, Satellite DNA, Centromere




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