Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.

Abstract:

:The fusion of inner mitochondrial membranes requires dynamin-like GTPases, Mgm1 in yeast and OPA1 in mammals, but how they mediate membrane fusion is poorly understood. Here, we determined the crystal structure of Saccharomyces cerevisiae short Mgm1 (s-Mgm1) in complex with GDP. It revealed an N-terminal GTPase (G) domain followed by two helix bundles (HB1 and HB2) and a unique C-terminal lipid-interacting stalk (LIS). Dimers can form through antiparallel HB interactions. Head-to-tail trimers are built by intermolecular interactions between the G domain and HB2-LIS. Biochemical and in vivo analyses support the idea that the assembly interfaces observed here are native and critical for Mgm1 function. We also found that s-Mgm1 interacts with negatively charged lipids via both the G domain and LIS. Based on these observations, we propose that membrane targeting via the G domain and LIS facilitates the in cis assembly of Mgm1, potentially generating a highly curved membrane tip to allow inner membrane fusion.

authors

Yan L,Qi Y,Ricketson D,Li L,Subramanian K,Zhao J,Yu C,Wu L,Sarsam R,Wong M,Lou Z,Rao Z,Nunnari J,Hu J

doi

10.1073/pnas.1919116117

subject

Has Abstract

pub_date

2020-02-25 00:00:00

pages

4061-4070

issue

8

eissn

0027-8424

issn

1091-6490

pii

1919116117

journal_volume

117

pub_type

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