Abstract：
:Bacterial actin MreB is one of the key components of the bacterial cytoskeleton. It assembles into short filaments that lie just underneath the membrane and organize the cell wall synthesis machinery. Here we show that MreB from both T. maritima and E. coli binds directly to cell membranes. This function is essential for cell shape determination in E. coli and is proposed to be a general property of many, if not all, MreBs. We demonstrate that membrane binding is mediated by a membrane insertion loop in TmMreB and by an N-terminal amphipathic helix in EcMreB and show that purified TmMreB assembles into double filaments on a membrane surface that can induce curvature. This, the first example of a membrane-binding actin filament, prompts a fundamental rethink of the structure and dynamics of MreB filaments within cells.
journal_name
Mol Celljournal_title
Molecular cellauthors
Salje J,van den Ent F,de Boer P,Löwe Jdoi
10.1016/j.molcel.2011.07.008subject
Has Abstractpub_date
2011-08-05 00:00:00pages
478-87issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(11)00530-2journal_volume
43pub_type
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