Other formats:
BibTeX
LaTeX
RIS
@article{2413672,
author = {Vaculíková, Jitka and Hola, Marcela and Králová, Barbora and Lelkes, Edit and Štefanovie, Barbora and Vagnerova, Radka and Angelis, Karel J. and Paleček, Jan},
article_location = {Hoboken (USA)},
article_number = {3},
doi = {http://dx.doi.org/10.1111/tpj.16869},
keywords = {Physcomitrium patens SMC5/6 complex; NSE5/SNI1/SLF1/SIMC1; NSE6/ASAP1/SLF2/KRE29; DNA damage repair; rDNA stability; moss caulonemata development},
language = {eng},
issn = {0960-7412},
journal = {Plant Journal},
title = {NSE5 subunit interacts with distant regions of the SMC arms in the <i>Physcomitrium patens</i> SMC5/6 complex},
url = {https://onlinelibrary.wiley.com/doi/10.1111/tpj.16869},
volume = {119},
year = {2024}
}
TY - JOUR
ID - 2413672
AU - Vaculíková, Jitka - Hola, Marcela - Králová, Barbora - Lelkes, Edit - Štefanovie, Barbora - Vagnerova, Radka - Angelis, Karel J. - Paleček, Jan
PY - 2024
TI - NSE5 subunit interacts with distant regions of the SMC arms in the <i>Physcomitrium patens</i> SMC5/6 complex
JF - Plant Journal
VL - 119
IS - 3
SP - 1481-1493
EP - 1481-1493
PB - Wiley-Blackwell
SN - 09607412
KW - Physcomitrium patens SMC5/6 complex
KW - NSE5/SNI1/SLF1/SIMC1
KW - NSE6/ASAP1/SLF2/KRE29
KW - DNA damage repair
KW - rDNA stability
KW - moss caulonemata development
UR - https://onlinelibrary.wiley.com/doi/10.1111/tpj.16869
N2 - Structural maintenance of chromosome (SMC) complexes play roles in cohesion, condensation, replication, transcription, and DNA repair. Their cores are composed of SMC proteins with a unique structure consisting of an ATPase head, long arm, and hinge. SMC complexes form long rod-like structures, which can change to ring-like and elbow-bent conformations upon binding ATP, DNA, and other regulatory factors. These SMC dynamic conformational changes are involved in their loading, translocation, and DNA loop extrusion. Here, we examined the binding and role of the PpNSE5 regulatory factor of Physcomitrium patens PpSMC5/6 complex. We found that the PpNSE5 C-terminal half (aa230-505) is required for binding to its PpNSE6 partner, while the N-terminal half (aa1-230) binds PpSMC subunits. Specifically, the first 71 amino acids of PpNSE5 were required for binding to PpSMC6. Interestingly, the PpNSE5 binding required the PpSMC6 head-proximal joint region and PpSMC5 hinge-proximal arm, suggesting a long distance between binding sites on PpSMC5 and PpSMC6 arms. Therefore, we hypothesize that PpNSE5 either links two antiparallel SMC5/6 complexes or binds one SMC5/6 in elbow-bent conformation, the later model being consistent with the role of NSE5/NSE6 dimer as SMC5/6 loading factor to DNA lesions. In addition, we generated the P. patens Ppnse5KO1 mutant line with an N-terminally truncated version of PpNSE5, which exhibited DNA repair defects while keeping a normal number of rDNA repeats. As the first 71 amino acids of PpNSE5 are required for PpSMC6 binding, our results suggest the role of PpNSE5-PpSMC6 interaction in SMC5/6 loading to DNA lesions.
ER -
VACULÍKOVÁ, Jitka, Marcela HOLA, Barbora KRÁLOVÁ, Edit LELKES, Barbora ŠTEFANOVIE, Radka VAGNEROVA, Karel J. ANGELIS and Jan PALEČEK. NSE5 subunit interacts with distant regions of the SMC arms in the \&{}lt;i\&{}gt;Physcomitrium patens\&{}lt;/i\&{}gt; SMC5/6 complex. \textit{Plant Journal}. Hoboken (USA): Wiley-Blackwell, 2024, vol.~119, No~3, p.~1481-1493. ISSN~0960-7412. Available from: https://dx.doi.org/10.1111/tpj.16869.
|
