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cDNA Library Screening Identifies Protein Interactors Potentially Involved in Non-Telomeric Roles of Arabidopsis Telomerase

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DOKLÁDAL Ladislav HONYS David RANA Rajiv LEE Lan-Ying GELVIN Stanton B. SÝKOROVÁ Eva

Rok publikování 2015
Druh Článek v odborném periodiku
Časopis / Zdroj Frontiers in Plant Science
Fakulta / Pracoviště MU

Středoevropský technologický institut

Obor Botanika
Klíčová slova telomerase; nuclear poly(A)-binding protein; telobox; metallothionein 2A; MODIFIER OF snc1; putative nuclear DNA-binding protein G2p; oxidation-related zinc finger 2 protein; BiFC
Popis Telomerase-reverse transcriptase (TERT) plays an essential catalytic role in maintaining telomeres. However, in animal systems telomerase plays additional non-telomeric functional roles. We previously screened an Arabidopsis cDNA library for proteins that interact with the C-terminal extension (CTE) TERT domain and identified a nuclearlocalized protein that contains an RNA recognition motif (RRM). This RRM-protein forms homodimers in both plants and yeast. Mutation of the gene encoding the RRM-protein had no detectable effect on plant growth and development, nor did it affect telomerase activity or telomere length in vivo, suggesting a non-telomeric role for TERT/RRM-protein complexes. The gene encoding the RRM-protein is highly expressed in leaf and reproductive tissues. We further screened an Arabidopsis cDNA library for proteins that interact with the RRM-protein and identified five interactors. These proteins are involved in numerous non-telomere-associated cellular activities. In plants, the RRM-protein, both alone and in a complex with its interactors, localizes to nuclear speckles. Transcriptional analyses in wild-type and rrm mutant plants, as well as transcriptional co-analyses, suggest that TERT, the RRM-protein, and the RRM-protein interactors may play important roles in non-telomeric cellular functions.
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