Journal
FEBS JOURNAL
Volume 276, Issue 14, Pages 4194-4207Publisher
WILEY
DOI: 10.1111/j.1742-4658.2009.07092.x
Keywords
Arg methylation; nuclear bodies; protein-protein interaction; RNA binding; splicing
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Funding
- Fundacao de Amparo a Pesquisa do Estado Sao Paulo (FAPESP)
- Conselho Nacional de Pesquisa e Desenvolvimento (CNPq)
- LNLS
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The cytoplasmic and nuclear protein Ki- 1 / 57 was first identified in malignant cells from Hodgkin's lymphoma. Despite studies showing its phosphorylation, arginine methylation, and interaction with several regulatory proteins, the functional role of Ki- 1 / 57 in human cells remains to be determined. Here, we investigated the relationship of Ki- 1 / 57 with RNA functions. Through immunoprecipitation assays, we verified the association of Ki- 1 / 57 with the endogenous splicing proteins hnRNPQ and SFRS9 in HeLa cell extracts. We also found that recombinant Ki- 1 / 57 was able to bind to a poly- U RNA probe in electrophoretic mobility shift assays. In a classic splicing test, we showed that Ki- 1 / 57 can modify the splicing site selection of the adenoviral E1A minigene in a dose- dependent manner. Further confocal and. uorescence microscopy analysis revealed the localization of enhanced green. uorescent protein - Ki- 1 / 57 to nuclear bodies involved in RNA processing and or small nuclear ribonucleoprotein assembly, depending on the cellular methylation status and its N- terminal region. In summary, our findings suggest that Ki- 1 / 57 is probably involved in cellular events related to RNA functions, such as pre- mRNA splicing.
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