Publication details
An armadillo-domain protein participates in a telomerase interaction network
| Authors | |
|---|---|
| Year of publication | 2018 |
| Type | Article in Periodical |
| Magazine / Source | Plant Molecular Biology |
| MU Faculty or unit | |
| Citation | |
| Web | https://link.springer.com/article/10.1007%2Fs11103-018-0747-4 |
| Doi | http://dx.doi.org/10.1007/s11103-018-0747-4 |
| Keywords | Armadillo/beta-catenin-like repeat; ARMC6; AtTERT; Homologous recombination; Protein–protein interaction; Telomerase activity |
| Description | 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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