Opis

• Tytuł:
  Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex
• Twórca:
  Wiedemann, Christoph;
  Szambowska, Anna;
  Häfner, Sabine;
  Ohlenschläger, Oliver;
  Gührs, Karl-Heinz;
  Görlach, Matthias
• Opis:
  The minichromosome maintenance complex (MCM) represents the replicative DNA helicase both in eukaryotes and archaea. Here, we describe the solution structure of the C-terminal domains of the archaeal MCMs of Sulfolobus solfataricus (Sso) and Methanothermobacter thermautotrophicus (Mth). Those domains consist of a structurally conserved truncated winged helix (WH) domain lacking the two typical 'wings' of canonical WH domains. A less conserved N-terminal extension links this WH module to the MCM AAA+ domain forming the ATPase center. In the Sso MCM this linker contains a short α-helical element. Using Sso MCM mutants, including chimeric constructs containing Mth C-terminal domain elements, we show that the ATPase and helicase activity of the Sso MCM is significantly modulated by the short α-helical linker element and by N-terminal residues of the first α-helix of the truncated WH module. Finally, based on our structural and functional data, we present a docking-derived model of the Sso MCM, which implies an allosteric control of the ATPase center by the C-terminal domain.
• Dostępność obiektu:
  Dostęp otwarty
• Data:
  2015
• Typ:
  Article;
  PeerReviewed
• Język:
  angielski
• Format:
  application/pdf
• Relacja: http://eprints.ibb.waw.pl/1043 ;http://nar.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=25712103
• Temat i słowa kluczowe:
  QH301 Biology;
  QH426 Genetics;
  QR Microbiology
• Identyfikator: http://eprints.ibb.waw.pl/1043/1/gkv120.pdf ;
  Wiedemann, Christoph and Szambowska, Anna and Häfner, Sabine and Ohlenschläger, Oliver and Gührs, Karl-Heinz and Görlach, Matthias (2015) Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex. Nucleic acids research, 43 (5). pp. 2958-2967. ISSN 1362-4962
• Dostawca danych:
  Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk
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