Abstract:
:The AAA+ ATPase Vps4 disassembles ESCRT-III and is essential for HIV-1 budding and other pathways. Vps4 is a paradigmatic member of a class of hexameric AAA+ ATPases that disassemble protein complexes without degradation. To distinguish between local displacement versus global unfolding mechanisms for complex disassembly, we carried out hydrogen/deuterium exchange during Saccharomyces cerevisiae Vps4 disassembly of a chimeric Vps24-2 ESCRT-III filament. EX1 exchange behavior shows that Vps4 completely unfolds ESCRT-III substrates on a time scale consistent with the disassembly reaction. The established unfoldase ClpX showed the same pattern, thus demonstrating a common unfolding mechanism. Vps4 hexamers containing a single cysteine residue in the pore loops were cross-linked to ESCRT-III subunits containing unique cysteines within the folded core domain. These data support a mechanism in which Vps4 disassembles its substrates by completely unfolding them and threading them through the central pore.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Yang B,Stjepanovic G,Shen Q,Martin A,Hurley JHdoi
10.1038/nsmb.3015subject
Has Abstractpub_date
2015-06-01 00:00:00pages
492-8issue
6eissn
1545-9993issn
1545-9985pii
nsmb.3015journal_volume
22pub_type
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