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The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.

Abstract：

:TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator. Also, it likely does not thread a peptide substrate through a narrow central channel, in contrast to its closest structural homologs. Here, we examined the oligomerization of TorsinA to get closer to a molecular understanding of its still enigmatic function. We observe TorsinA to form helical filaments, which we analyzed by cryo-electron microscopy using helical reconstruction. The 4.4 Å structure reveals long hollow tubes with a helical periodicity of 8.5 subunits per turn, and an inner channel of ~ 4 nm diameter. We further show that the protein is able to induce tubulation of membranes in vitro, an observation that may reflect an entirely new characteristic of AAA + ATPases. We discuss the implications of these observations for TorsinA function.

journal_name

Nat Commun

journal_title

Nature communications

authors

Demircioglu FE,Zheng W,McQuown AJ,Maier NK,Watson N,Cheeseman IM,Denic V,Egelman EH,Schwartz TU

doi

10.1038/s41467-019-11194-w

subject

Has Abstract

pub_date

2019-07-22 00:00:00

pages

3262

issue

1

issn

2041-1723

pii

10.1038/s41467-019-11194-w

journal_volume

10

pub_type

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