<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Dokládal, Ladislav</dc:creator>
  <dc:creator>Benková, Eva</dc:creator>
  <dc:creator>Honys, David</dc:creator>
  <dc:creator>Dupláková, Nikoleta</dc:creator>
  <dc:creator>Lee, Lan-Ying</dc:creator>
  <dc:creator>Gelvin, Stanton B.</dc:creator>
  <dc:creator>Sýkorová, Eva</dc:creator>
  <dc:date>2018-07-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">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.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/307377</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307377/files/dok_adp.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307377/files/dok_adp_sm.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307377/files/dok_adp_sm1.txt</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307377/files/dok_adp_sm2.txt</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1007/s11103-018-0747-4</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Plant Molecular Biology. - 2018, vol. 97, no. 4, p. 407–420</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">An armadillo-domain protein participates in a telomerase interaction network</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
