Structures and mechanisms of AAA+ protein complexes in DNA processing
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Updated: May 12, 2025

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
Published on: March 9, 2022
Alexander Carver1, Bowen Zhang1, Xiaodong Zhang1
1Section of Structural and Synthetic Biology, Faculty of Medicine, Imperial College London, South Kensington, London, SW7 2AZ, UK; Laboratory of DNA Processing Machines, The Francis Crick Institute, London, NW1 1AT, UK.
Abstract:
AAA+ proteins are a large family of ATPases involved in a myriad of cellular activities. Recent advances in AAA+ proteins, especially cryoEM structures of these proteins in complex with their substrates, have provided key insights into how they function. Here we review recent progress in structural studies and mechanistic understanding of AAA+ proteins involved in DNA processing, including gene transcription, DNA replication, repair/recombination and transposition. Using a few selected examples, we show how AAA+ proteins act on both DNA and protein peptides, which are often enclosed in the pores of AAA+ hexamers. We propose that using AAA+ proteins to translocate a peptide to partially unfold a substrate is an effective strategy in disassembling an assembled complex. Further, several studies show that although they often act as asymmetric hexamers in their active form, AAA+ proteins adopt a range of oligomers for their functions.
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