Understanding how biological membranes are shaped by coupling proteins to membranes: biophysical basis for the function of pairs of dynamin-like proteins in the bacterial pathogen Helicobacter Pylori
Abstract
Life depends on the compartmentalization of molecules and biological processes. This partitioning is maintained largely by the use of lipid membranes and by a number of protein families that shape membranes. This project will focus on the dynamin-super family, which is found in all domains of life, that plays central roles in the shaping, fusing and scission of membranes. In mammals, the archetypal Dynamin 1 binds to membranes, forming a helical polymer that upon constriction causes membrane scission. In bacteria the roles of dynamin-like proteins are not yet understood. Bacterial dynamins are structurally similar to eukaryotic dynamins however there are some marked differences. Intriguingly bacterial dynamin-like proteins are encoded in pairs. The reason for this is unknown.
Document Details
- Document Type
- DoD Grant Award
- Publication Date
- Nov 16, 2022
- Source ID
- FA23862114019
Entities
People
- Katharine A Michie
Organizations
- Air Force Office of Scientific Research
- United States Air Force
- University of New South Wales