인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
The minichromosome maintenance (MCM) complex is the replicative helicase in eukaryotes and archaea, unwinding genomic DNA upstream of DNA polymerase. The eukaryotic MCM complex forms from six different subunits (Mcm2-7), whereas in archaea, the complex is homohexameric. Both types of MCM can assemble into functional helicases in vitro in the absence of cofactors. However, despite being simpler in composition, we know little about how a homohexameric archaeal MCM assembles, largely because the field has lacked a convenient system to interrogate. Historically, characterization of archaeal MCMs has focused on proteins from thermophilic organisms, which typically form robust oligomers in solution. We have identified an uncharacterized MCM from the mesophilic archaeon Mancarchaeum acidophilum (MacMCM) that shows strong DNA unwinding activity at room temperature. Unexpectedly, apo-MacMCM is monomeric in solution, providing a first opportunity to investigate the mechanisms of assembly of an active homohexameric MCM complex in vitro. We show that MacMCM requires both ATP and DNA to form an active homohexamer, and that the C-terminal winged-helix domain impedes oligomerization. We report the 3D structure of MacMCM, which reveals similar numbers of interactions at subunit-subunit interfaces as eukaryotic MCMs but fewer than MCMs from thermophilic archaea. Finally, we show that installing subunit-subunit salt bridges from Sulfolobus solfataricus MCM into MacMCM promotes oligomerization. Heterohexameric eukaryotic MCMs evolved from a homomeric ancestor. Our results identify structural and ligand-driven mechanisms of assembly that are conserved between homomeric and heteromeric MCMs.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.