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Lookup NU author(s): Dr Sven Halbedel, Dr Leendert Hamoen
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DivIVA is a conserved protein in Gram-positive bacteria that localizes at the poles and division sites, presumably through direct sensing of membrane curvature. DivIVA functions as a scaffold and is vital for septum site selection during vegetative growth and chromosome anchoring during sporulation. DivIVA deletion causes filamentous growth in Bacillus subtilis, whereas overexpression causes hyphal branching in Streptomyces coelicolor. We have determined the crystal structure of the N-terminal (Nt) domain of DivIVA, and show that it forms a parallel coiled-coil. It is capped with two unique crossed and intertwined loops, exposing hydrophobic and positively charged residues that we show here are essential for membrane binding. An intragenic suppressor introducing a positive charge restores membrane binding after mutating the hydrophobic residues. We propose that the hydrophobic residues insert into the membrane and that the positively charged residues bind to the membrane surface. A low-resolution crystal structure of the C-terminal (Ct) domain displays a curved tetramer made from two parallel coiled-coils. The Nt and Ct parts were then merged into a model of the full length, 30 nm long DivIVA protein. The EMBO Journal (2010) 29, 1988-2001. doi: 10.1038/emboj.2010.99; Published online 25 May 2010
Author(s): Oliva MA, Halbedel S, Freund SM, Dutow P, Leonard TA, Veprintsev DB, Hamoen LW, Lowe J
Publication type: Article
Publication status: Published
Journal: EMBO Journal
Year: 2010
Volume: 29
Issue: 12
Pages: 1988-2001
Print publication date: 01/06/2010
ISSN (print): 0261-4189
ISSN (electronic): 1460-2075
Publisher: Nature Publishing Group
URL: http://dx.doi.org/10.1038/emboj.2010.99
DOI: 10.1038/emboj.2010.99
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