Detailed Information on Publication Record
2023
Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens PpSMC5/6 complex
LELKES, Edit, Jitka JEMELKOVÁ, Marcela HOLÁ, Barbora ŠTEFANOVIE, Peter KOLESÁR et. al.Basic information
Original name
Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens PpSMC5/6 complex
Name in Czech
Charakterizace konzervovaných vlastností NSE6 podjednotky Physcomitrium patens komplexu PpSMC5/6
Authors
LELKES, Edit (703 Slovakia, belonging to the institution), Jitka JEMELKOVÁ (203 Czech Republic, belonging to the institution), Marcela HOLÁ (203 Czech Republic), Barbora ŠTEFANOVIE (703 Slovakia, belonging to the institution), Peter KOLESÁR (703 Slovakia, belonging to the institution), Radka VÁGNEROVÁ (203 Czech Republic), Eva DVOŘÁK TOMAŠTÍKOVÁ (203 Czech Republic), Aleš PEČINKA (203 Czech Republic), Karel J. ANGELIS (203 Czech Republic) and Jan PALEČEK (203 Czech Republic, guarantor, belonging to the institution)
Edition
PLANT JOURNAL, ENGLAND, WILEY, 2023, 0960-7412
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 7.200 in 2022
RIV identification code
RIV/00216224:14310/23:00132792
Organization unit
Faculty of Science
UT WoS
000995683100001
Keywords in English
SMC5/6 complex; NSE5/SNI1/SLF1/SIMC1; NSE6/ASAP1/SLF2/KRE29; CANIN domain; DNA damage repair; plant development; Physcomitrium patens
Tags
International impact, Reviewed
Změněno: 19/1/2024 10:43, Mgr. Marie Šípková, DiS.
Abstract
V originále
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.
Links
GA20-05095S, research and development project |
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LM2018129, research and development project |
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MUNI/R/1142/2021, interní kód MU |
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MUNI/R/1262/2022, interní kód MU |
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