Telomere repeat binding proteins are functional components of <scp>A</scp>rabidopsis telomeres and interact with telomerase

Schrumpfová, Petra Procházková; Vychodilová, Ivona; Dvořáčková, Martina; Majerská, Jana; Dokládal, Ladislav; Schořová, Šárka; Fajkus, Jiřı́

doi:10.1111/tpj.12428

Cited by 59 publications

(72 citation statements)

References 72 publications

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“…In contrast, sorghum, rice, and maize show non-Rabl patterns. In the case of tobacco, the telomeres are localized at random in the nucleus in a typical non-Rabl pattern (Fujimoto et al 2005, Lee and Kim 2013, Schrumpfová et al 2014. The signal pattern observed with dCas9-FP for telomeres was similar to previous telomere localization patterns in tobacco.…”

Section: Transient Expression Of Dcas9-fp and Sgrna For Telomeres In supporting

confidence: 84%

Visualization of Chromatin Loci with Transiently Expressed CRISPR/Cas9 in Plants

Fujimoto

Matsunaga

2017

CYTOLOGIA

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Labeling of specific DNA sequences in living organisms is important for understanding the mechanism of gene regulation during development, differentiation, and environmental adaptation. Here we describe a CRISPR/Cas9-based chromatin visualization system in plants. We adapted the mammalian nuclease-dead Cas9fluorescent protein (dCas9-FP) system to a plant expression vector. Transient expression of dCas9-FP and single guide RNA (sgRNA) for telomeric sequences efficiently labeled telomere repeats in tobacco.

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Section: Transient Expression Of Dcas9-fp and Sgrna For Telomeres In supporting

confidence: 84%

Visualization of Chromatin Loci with Transiently Expressed CRISPR/Cas9 in Plants

Fujimoto

Matsunaga

2017

CYTOLOGIA

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“…PRR:GFP was immunoprecipitated with an antibody against GFP and for each PRR a HA:CO co‐immunoprecipitation could be observed (Fig 5C). By contrast, HA:CO was not precipitated by the GFP antibody when 35S: HA:CO was infiltrated alone or with 35S:: TRB3:YFP , which expresses a fusion of TELOMERE REPEAT BINDING 3 fused to YFP (Figs 5C and EV5A; Schrumpfova et al , 2014; Zhou et al , 2016). In summary, these results indicate that each PRR can physically interact with CO in planta .…”

Section: Resultsmentioning

confidence: 98%

PSEUDO RESPONSE REGULATORs stabilize CONSTANS protein to promote flowering in response to day length

et al. 2017

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Seasonal reproduction in many organisms requires detection of day length. This is achieved by integrating information on the light environment with an internal photoperiodic time‐keeping mechanism. Arabidopsis thaliana promotes flowering in response to long days (LDs), and CONSTANS (CO) transcription factor represents a photoperiodic timer whose stability is higher when plants are exposed to light under LDs. Here, we show that PSEUDO RESPONSE REGULATOR (PRR) proteins directly mediate this stabilization. PRRs interact with and stabilize CO at specific times during the day, thereby mediating its accumulation under LDs. PRR‐mediated stabilization increases binding of CO to the promoter of FLOWERING LOCUS T (FT), leading to enhanced FT transcription and early flowering under these conditions. PRRs were previously reported to contribute to timekeeping by regulating CO transcription through their roles in the circadian clock. We propose an additional role for PRRs in which they act upon CO protein to promote flowering, directly coupling information on light exposure to the timekeeper and allowing recognition of LDs.

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“…TRB1 (AT1G49950), TRB2 (AT5G67580), and TRP1 (AT5G59430) constructs in pGADT7 and pGBKT7 vectors were prepared previously (Kuchar and Fajkus 2004). Each bait/prey combination was co-transformed into Saccharomyces cerevisiae PJ69-4a and Y2H analysis was performed as described in (Schrumpfova et al 2014) using TRB1-RID interaction as a positive control. Protein expression was verified by immunoblotting using mouse anti-HA (kindly provided by Bořivoj Vojtěšek, Masaryk university Brno, Czech Republic) or mouse anti-myc primary antibodies and a HRP-conjugated anti-mouse secondary antibody (both Sigma-Aldrich, http://www.sigma -aldri ch.com) (Supplemental Fig.…”

Section: Yeast Two Hybrid (Y2h) and Co-immunoprecipitation (Co-ip) Anmentioning

confidence: 99%

“…Prey proteins were radioactively labeled using 35 S-Met (Hartmann Analytic, Germany). The co-IP procedure was performed as described by Schrumpfova et al (2014) using mouse anti-myc antibody (9E10, Sigma) and magnetic beads Dynabeads® Protein G (Life Technologies, https ://www.therm ofish er.com). Proteins in input, unbound, and bound fractions were separated by 12.5% SDS-PAGE, blotted onto Amersham Hybond-ECL membranes (GE Healthcare, http://www.gelif escie nces.com/), and analyzed using an FLA7000 imager (Fujifilm).…”

Section: Yeast Two Hybrid (Y2h) and Co-immunoprecipitation (Co-ip) Anmentioning

confidence: 99%

“…However any function of these proteins in telomere maintenance has not previously been demonstrated (Fulcher and Riha 2015). Telomeric functions in vivo were recently demonstrated for the plant-specific Single Myb Histone (SMH) proteins (Dvorackova et al 2015;Schrumpfova et al 2014). Moreover, the SMH proteins may function as chromatin modulators: they bind promoter regions of genes involved in ribosome biogenesis (Schrumpfova et al 2016;Zhou et al 2016) and of other genes containing a telobox, a regulatory motif with a sequence identical to that of the plant telomeric repeat (AAA CCC T)n (Regad et al 1994).…”

Section: Introductionmentioning

confidence: 99%

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An armadillo-domain protein participates in a telomerase interaction network

et al. 2018

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Arabidopsis 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. Telomerase 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.

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Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase

Cited by 59 publications

References 72 publications

Visualization of Chromatin Loci with Transiently Expressed CRISPR/Cas9 in Plants

Visualization of Chromatin Loci with Transiently Expressed CRISPR/Cas9 in Plants

PSEUDO RESPONSE REGULATORs stabilize CONSTANS protein to promote flowering in response to day length

An armadillo-domain protein participates in a telomerase interaction network

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