Počet záznamů: 1
Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex
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SYSNO ASEP 0575938 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex Tvůrce(i) Lelkes, E. (CZ)
Jemelková, J. (CZ)
Holá, Marcela (UEB-Q) ORCID
Štefanovie, B. (CZ)
Kolesár, P. (CZ)
Vágnerová, Radka (UEB-Q) ORCID
Tomaštíková, Eva (UEB-Q) RID, ORCID
Pečinka, Aleš (UEB-Q) ORCID, RID
Angelis, Karel (UEB-Q) RID, ORCID
Paleček, J. J. (CZ)Celkový počet autorů 10 Zdroj.dok. Plant Journal. - : Wiley - ISSN 0960-7412
Roč. 115, č. 4 (2023), s. 1084-1099Poč.str. 16 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova CANIN domain ; DNA damage repair ; nse5/sni1/slf1/simc1 ; nse6/asap1/slf2/kre29 ; Physcomitrium patens ; plant development ; SMC5/6 complex Obor OECD Plant sciences, botany CEP LM2018129 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA20-05095S GA ČR - Grantová agentura ČR GA22-00871S GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora UEB-Q - RVO:61389030 UT WOS 000995683100001 EID SCOPUS 85160655391 DOI 10.1111/tpj.16282 Anotace 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. Pracoviště Ústav experimentální botaniky Kontakt David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Rok sběru 2024 Elektronická adresa https://doi.org/10.1111/tpj.16282
Počet záznamů: 1