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2017 | 64 | 1 | 177-181

Article title

Human SUV3 helicase regulates growth rate of the HeLa cells and can localize in the nucleoli

Content

Title variants

Languages of publication

EN

Abstracts

EN
The human SUV3 helicase (SUV3, hSUV3, SUPV3L1) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome with exonuclease PNP (polynucleotide phosphorylase). Association of this complex with the polyA polymerase can modulate mitochondrial polyA tails. Silencing of the SUV3 gene was shown to inhibit the cell cycle and to induce apoptosis in human cell lines. However, since small amounts of the SUV3 helicase were found in the cell nuclei, it was not clear whether the observed phenotypes of SUV3 depletion were of mitochondrial or nuclear origin. In order to answer this question we have designed gene constructs able to inhibit the SUV3 activity exclusively in the cell nuclei. The results indicate that the observed growth rate impairment upon SUV3 depletion is due to its nuclear function(s). Unexpectedly, overexpression of the nuclear-targeted wild-type copies of the SUV3 gene resulted in a higher growth rate. In addition, we demonstrate that the SUV3 helicase can be found in the HeLa cell nucleoli, but it is not detectable in the DNA-repair foci. Our results indicate that the nucleolar-associated human SUV3 protein is an important factor in regulation of the cell cycle.

Year

Volume

64

Issue

1

Pages

177-181

Physical description

Dates

published
2017
received
2016-09-02
revised
2017-01-13
accepted
2017-01-16
(unknown)
2017-03-15

Contributors

  • Institute of Genetics and Biotechnology, Faculty of Biology, Warsaw University, Warsaw, Poland
  • Centre for New Technologies, University of Warsaw, Warsaw, Poland
  • Institute of Genetics and Biotechnology, Faculty of Biology, Warsaw University, Warsaw, Poland
  • Department of Cell Biophysics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
  • Department of Cell Biophysics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
  • Institute of Genetics and Biotechnology, Faculty of Biology, Warsaw University, Warsaw, Poland
  • Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warsaw, Poland
  • Centre for New Technologies, University of Warsaw, Warsaw, Poland

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv64p177kz
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