Structure and function of bacterial dynamin-like proteins.

Abstract:

:Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis to membrane deformation, which eventually leads to fusion or fission of the lipid bilayer. Mutations in eukaryotic dynamin-like proteins (DLPs) are associated with various diseases underscoring the importance to fully understand the biochemistry of these proteins. In recent years, a wealth of structural and biochemical data have been published that allow a detailed analysis of how dynamins or DLPs modulate biological membranes. However, less is known about the function of bacterial DLPs, although structural data exist. This review summarizes current knowledge about bacterial dynamins and discusses structural and functional properties in comparison to their eukaryotic counterparts.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Bramkamp M

doi

10.1515/hsz-2012-0185

subject

Has Abstract

pub_date

2012-11-01 00:00:00

pages

1203-14

issue

11

eissn

1431-6730

issn

1437-4315

pii

/j/bchm.2012.393.issue-11/hsz-2012-0185/hsz-2012-0

journal_volume

393

pub_type

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