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@article{2356460,
author = {Lelkes, Edit and Jemelková, Jitka and Holá, Marcela and Štefanovie, Barbora and Kolesár, Peter and Vágnerová, Radka and Dvořák Tomaštíková, Eva and Pečinka, Aleš and Angelis, Karel J. and Paleček, Jan},
article_location = {ENGLAND},
article_number = {4},
doi = {http://dx.doi.org/10.1111/tpj.16282},
keywords = {SMC5/6 complex; NSE5/SNI1/SLF1/SIMC1; NSE6/ASAP1/SLF2/KRE29; CANIN domain; DNA damage repair; plant development; Physcomitrium patens},
language = {eng},
issn = {0960-7412},
journal = {PLANT JOURNAL},
title = {Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens PpSMC5/6 complex},
url = {https://onlinelibrary.wiley.com/doi/10.1111/tpj.16282},
volume = {115},
year = {2023}
}
TY - JOUR
ID - 2356460
AU - Lelkes, Edit - Jemelková, Jitka - Holá, Marcela - Štefanovie, Barbora - Kolesár, Peter - Vágnerová, Radka - Dvořák Tomaštíková, Eva - Pečinka, Aleš - Angelis, Karel J. - Paleček, Jan
PY - 2023
TI - Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens PpSMC5/6 complex
JF - PLANT JOURNAL
VL - 115
IS - 4
SP - 1084-1099
EP - 1084-1099
PB - WILEY
SN - 09607412
KW - SMC5/6 complex
KW - NSE5/SNI1/SLF1/SIMC1
KW - NSE6/ASAP1/SLF2/KRE29
KW - CANIN domain
KW - DNA damage repair
KW - plant development
KW - Physcomitrium patens
UR - https://onlinelibrary.wiley.com/doi/10.1111/tpj.16282
N2 - 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.
ER -
LELKES, Edit, Jitka JEMELKOVÁ, Marcela HOLÁ, Barbora ŠTEFANOVIE, Peter KOLESÁR, Radka VÁGNEROVÁ, Eva DVOŘÁK TOMAŠTÍKOVÁ, Aleš PEČINKA, Karel J. ANGELIS and Jan PALEČEK. Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens PpSMC5/6 complex. \textit{PLANT JOURNAL}. ENGLAND: WILEY, 2023, vol.~115, No~4, p.~1084-1099. ISSN~0960-7412. Available from: https://dx.doi.org/10.1111/tpj.16282.
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