Completing the TRB family: newly characterized members show ancient evolutionary origins and distinct localization, yet similar interactions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F23%3A00575345" target="_blank" >RIV/61389030:_____/23:00575345 - isvavai.cz</a>
Alternative codes found
RIV/60077344:_____/23:00575345 RIV/00216224:14310/23:00132876 RIV/00216208:11310/23:10475595
Result on the web
<a href="https://doi.org/10.1007/s11103-023-01348-2" target="_blank" >https://doi.org/10.1007/s11103-023-01348-2</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s11103-023-01348-2" target="_blank" >10.1007/s11103-023-01348-2</a>
Alternative languages
Result language
angličtina
Original language name
Completing the TRB family: newly characterized members show ancient evolutionary origins and distinct localization, yet similar interactions
Original language description
Telomere repeat binding proteins (TRBs) belong to a family of proteins possessing a Myb-like domain which binds to telomeric repeats. Three members of this family (TRB1, TRB2, TRB3) from Arabidopsis thaliana have already been described as associated with terminal telomeric repeats (telomeres) or short interstitial telomeric repeats in gene promoters (telo-boxes). They are also known to interact with several protein complexes: telomerase, Polycomb repressive complex 2 (PRC2) E(z) subunits and the PEAT complex (PWOs-EPCRs-ARIDs-TRBs). Here we characterize two novel members of the TRB family (TRB4 and TRB5). Our wide phylogenetic analyses have shown that TRB proteins evolved in the plant kingdom after the transition to a terrestrial habitat in Streptophyta, and consequently TRBs diversified in seed plants. TRB4-5 share common TRB motifs while differing in several others and seem to have an earlier phylogenetic origin than TRB1-3. Their common Myb-like domains bind long arrays of telomeric repeats in vitro, and we have determined the minimal recognition motif of all TRBs as one telo-box. Our data indicate that despite the distinct localization patterns of TRB1-3 and TRB4-5 in situ, all members of TRB family mutually interact and also bind to telomerase/PRC2/PEAT complexes. Additionally, we have detected novel interactions between TRB4-5 and EMF2 and VRN2, which are Su(z)12 subunits of PRC2.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10611 - Plant sciences, botany
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Plant Molecular Biology
ISSN
0167-4412
e-ISSN
1573-5028
Volume of the periodical
112
Issue of the periodical within the volume
1-2
Country of publishing house
DE - GERMANY
Number of pages
23
Pages from-to
61-83
UT code for WoS article
000978294100001
EID of the result in the Scopus database
2-s2.0-85153708655