Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae.

Scientific Reports
Tomas HosekJean-Pierre Simorre

Abstract

MapZ localizes at midcell and acts as a molecular beacon for the positioning of the cell division machinery in the bacterium Streptococcus pneumoniae. MapZ contains a single transmembrane helix that separates the C-terminal extracellular domain from the N-terminal cytoplasmic domain. Only the structure and function of the extracellular domain is known. Here, we demonstrate that large parts of the cytoplasmic domain is intrinsically disordered and that there are two regions (from residues 45 to 68 and 79 to 95) with a tendency to fold into amphipathic helices. We further reveal that these regions interact with the surface of liposomes that mimic the Streptococcus pneumoniae cell membrane. The highly conserved and unfolded N-terminal region (from residues 17 to 43) specifically interacts with FtsZ independently of FtsZ polymerization state. Moreover, we show that MapZ phosphorylation at positions Thr67 and Thr68 does not impact the interaction with FtsZ or liposomes. Altogether, we propose a model in which the MapZ-mediated recruitment of FtsZ to mid-cell is modulated through competition of MapZ binding to the cell membrane. The molecular interplay between the components of this tripartite complex could represent a key step towar...Continue Reading

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Methods Mentioned

BETA
Nuclear Magnetic Resonance
NMR
electron microscopy
size exclusion chromatography
electrophoresis
light scattering

Software Mentioned

Consurf
Heliquest
Bruker
BEST
TROSY
Bruker Topspin
MapZ
CcpNmr
TopSpin
CcpNmr Analysis

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