An armadillo-domain protein participates in a telomerase interaction network

Dokládal, Ladislav; Benková, Eva; Honys, David; Dupláková, Nikoleta; Lee, Lan-Ying; Gelvin, Stanton B.; Sýkorová, Eva

doi:10.1007/s11103-018-0747-4

Back

Journal article

+ 3 other files

An armadillo-domain protein participates in a telomerase interaction network

Dokládal, Ladislav Institute of Biophysics, The Czech Academy of Sciences, Brno, Czech Republic - Laboratory of Functional Genomics and Proteomics, NCBR, Faculty of Science, Masaryk University, Brno, Czech Republic - Department of Biology, Faculty of Science and Medicine, University of Fribourg, Switzerland
Benková, Eva Institute of Science and Technology Austria, Klosterneuburg, Austria
Honys, David Institute of Experimental BotanyThe Czech Academy of Sciences, Prague, Czech Republic
Dupláková, Nikoleta Institute of Experimental BotanyThe Czech Academy of Sciences, Prague, Czech Republic
Lee, Lan-Ying Department of Biological SciencesPurdue University, West Lafayette, USA
Gelvin, Stanton B. Department of Biological SciencesPurdue University, West Lafayette, USA
Sýkorová, Eva Institute of Biophysics, The Czech Academy of Sciences, Brno, Czech Republic

01.07.2018

Published in:

Plant Molecular Biology. - 2018, vol. 97, no. 4, p. 407–420

English Key messageArabidopsis and human ARM protein interact with telomerase. Deregulated mRNA levels of DNA repair and ribosomal protein genes in an Arabidopsis arm mutant suggest non-telomeric ARM function. The human homolog ARMC6 interacts with hTRF2.AbstractTelomerase maintains telomeres and has proposed non-telomeric functions. We previously identified interaction of the C- terminal domain of Arabidopsis telomerase reverse transcriptase (AtTERT) with an armadillo/β-catenin-like repeat (ARM) containing protein. Here we explore protein– protein interactions of the ARM protein, AtTERT domains, POT1a, TRF-like family and SMH family proteins, and the chromatin remodeling protein CHR19 using bimolecular fluorescence complementation (BiFC), yeast two-hybrid (Y2H) analysis, and co- immunoprecipitation. 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.

Faculty

Faculté des sciences et de médecine

Department

Département de Biologie

Language