Characterization of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex

JEMELKOVÁ, Jitka, Edit LELKES, Marcela HOLÁ, Barbora ŠTEFANOVIE, Peter KOLESÁR, Karel J. ANGELIS and Jan PALEČEK. Characterization of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex. 2022.

Basic information

• Original name: Characterization of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex
• Authors: JEMELKOVÁ, Jitka, Edit LELKES, Marcela HOLÁ, Barbora ŠTEFANOVIE, Peter KOLESÁR, Karel J. ANGELIS and Jan PALEČEK.
• Edition: 2022.

Other information

• Original language: English
• Type of outcome: Conference abstract
• Field of Study: 10700 1.7 Other natural sciences
• Country of publisher: United Kingdom of Great Britain and Northern Ireland
• Confidentiality degree: is not subject to a state or trade secret
• Organization unit: Faculty of Science
• Tags: International impact

Abstract

Structural Maintenance of Chromosome (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 KITE or HAWK subunits. Additional NSE5 and NSE6 regulatory subunits interact with both SMC5 and SMC6 arms. Although their amino acid sequences are poorly conserved across the species, their primary function is to target SMC5/6 to the DNA damage sites. To characterize the NSE6 subunit of moss Physcomitrium patens, we analyzed its protein-protein interactions and Ppnse6 mutant phenotypes. In the human HsNSE6, we recently identified a new CANIN (for Coiled-coil SMC6 And NSE5 INteracting) domain. To further explore the conservation of this domain, we tracked down its sequence homology to lower plants and characterized its most conserved motif required for binding to its NSE5 partner. In addition, the CANIN domain and its preceding sequences bind and link SMC5 and SMC6 arms, suggesting its role in SMC5/6 dynamics. We hypothesized that this bridging of SMC5-SMC6 arms might negatively impact their dynamics, e.g. by limiting the opening of the SMC5/6 ring upon ATP binding.

Links

• GA20-05095S, research and development project: Name: Úloha komplexu SMC5/6 a jeho interakčních partnerů v opravě poškozené DNA (Acronym: SMC5/6)

Investor: Czech Science Foundation