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An armadillo-domain protein participates in a telomerase interaction network

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DOKLÁDAL Ladislav FRIMLOVÁ Eva HONYS David DUPĽÁKOVÁ Nikoleta LEE Lan-Ying GELVIN Stanton B. SÝKOROVÁ Eva

Rok publikování 2018
Druh Článek v odborném periodiku
Časopis / Zdroj Plant Molecular Biology
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www https://link.springer.com/article/10.1007%2Fs11103-018-0747-4
Doi http://dx.doi.org/10.1007/s11103-018-0747-4
Klíčová slova Armadillo/beta-catenin-like repeat; ARMC6; AtTERT; Homologous recombination; Protein–protein interaction; Telomerase activity
Popis The ARM protein interacts with both the N- and C-terminal domains of AtTERT in different cellular compartments. ARM interacts with CHR19 and TRF-like I family proteins that also bind AtTERT directly or through interaction with POT1a. The putative human ARM homolog co-precipitates telomerase activity and interacts with hTRF2 protein in vitro. Analysis of Arabidopsis arm mutants shows no obvious changes in telomere length or telomerase activity, suggesting that ARM is not essential for telomere maintenance. The observed interactions with telomerase and Myb-like domain proteins (TRF-like family I) may therefore reflect possible non-telomeric functions. Transcript levels of several DNA repair and ribosomal genes are affected in arm mutants, and ARM, likely in association with other proteins, suppressed expression of XRCC3 and RPSAA promoter constructs in luciferase reporter assays. In conclusion, ARM can participate in non-telomeric functions of telomerase, and can also perform its own telomerase-independent functions.
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