By the same authors

AAA(+) superfamily ATPases: common structure-diverse function

Research output: Contribution to journalLiterature review

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Publication details

JournalGENES TO CELLS
DatePublished - Jul 2001
Issue number7
Volume6
Number of pages23
Pages (from-to)575-597
Original languageEnglish

Abstract

The AAA(+) superfamily of ATPases, which contain a homologous ATPase module, are found in an kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring-shaped oligomers, which are crucial for their ATPase activities and mechanisms of action. These ring-shaped oligomeric complexes are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure; unfolding of proteins, disassembly of protein complexes, unwinding of DNA, or alteration of the state of DNA-protein complexes. Thus, the AAA(+) proteins represent a novel type of molecular chaperone. Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA(+) ATPases and other ring-shaped ATPases.

    Research areas

  • ATP-DEPENDENT PROTEASES, DNA-POLYMERASE-III, MEMBRANE-PROTEIN DEGRADATION, FTSH-MEDIATED PROTEOLYSIS, SENSITIVE FUSION PROTEIN, CHAPERONE-LIKE ACTIVITY, CELL-CYCLE PROGRESSION, REPLICATION-FACTOR-C, ESCHERICHIA-COLI, CRYSTAL-STRUCTURE

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