Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens PpSMC5/6 complex

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
Název česky Charakterizace konzervovaných vlastností NSE6 podjednotky Physcomitrium patens komplexu PpSMC5/6
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LELKES Edit JEMELKOVÁ Jitka HOLÁ Marcela ŠTEFANOVIE Barbora KOLESÁR Peter VÁGNEROVÁ Radka DVOŘÁK TOMAŠTÍKOVÁ Eva PEČINKA Aleš ANGELIS Karel J. PALEČEK Jan

Rok publikování 2023
Druh Článek v odborném periodiku
Časopis / Zdroj PLANT JOURNAL
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www https://onlinelibrary.wiley.com/doi/10.1111/tpj.16282
Doi http://dx.doi.org/10.1111/tpj.16282
Klíčová slova SMC5/6 complex; NSE5/SNI1/SLF1/SIMC1; NSE6/ASAP1/SLF2/KRE29; CANIN domain; DNA damage repair; plant development; Physcomitrium patens
Popis Structural maintenance of chromosomes (SMC) complexes are molecular machines ensuring chromatin organization at higher levels. They play direct roles in cohesion, condensation, replication, transcription, and DNA repair. Their cores are composed of long-armed SMC, kleisin, and kleisin-associated subunits. Additional factors, like NSE6 within SMC5/6, bind to SMC core complexes and regulate their activities. In the human HsNSE6/SLF2, we recently identified a new CANIN domain. Here we tracked down its sequence homology to lower plants, selected the bryophyte Physcomitrium patens, and analyzed PpNSE6 protein-protein interactions to explore its conservation in detail. We identified a previously unrecognized core sequence motif conserved from yeasts to humans within the NSE6 CANIN domain. This motif mediates the interaction between NSE6 and its NSE5 partner in yeasts and plants. In addition, the CANIN domain and its preceding PpNSE6 sequences bind both PpSMC5 and PpSMC6 arms. Interestingly, we mapped the PpNSE6-binding site at the PpSMC5 arm right next to the PpNSE2-binding surface. The position of NSE6 at SMC arms suggests its role in the regulation of SMC5/6 dynamics. Consistent with the regulatory role of NSE6 subunits, Ppnse6 mutant lines were viable and sensitive to the DNA-damaging drug bleomycin and lost a large portion of rDNA copies. These moss mutants also exhibited reduced growth and developmental aberrations. Altogether, our data showed the conserved function of the NSE6 subunit and architecture of the SMC5/6 complex across species.
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