SpoVID functions as a non-competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis

Molecular Microbiology
Filipa NunesAdriano O Henriques

Abstract

During sporulation in Bacillus subtilis, a group of mother cell-specific proteins guides the assembly of the coat, a multiprotein structure that protects the spore and influences many of its environmental interactions. SafA and CotE behave as party hubs, governing assembly of the inner and outer coat layers. Targeting of coat proteins to the developing spore is followed by encasement. Encasement by SafA and CotE requires E, a region of 11 amino acids in the encasement protein SpoVID, with which CotE interacts directly. Here, we identified two single alanine substitutions in E that prevent binding of SafA, but not of CotE, to SpoVID, and block encasement. The substitutions result in the accumulation of SafA, CotE and their dependent proteins at the mother cell proximal spore pole, phenocopying a spoVID null mutant and suggesting that mislocalized SafA acts as an attractor for the rest of the coat. The requirement for E in SafA binding is bypassed by a peptide with the sequence of E provided in trans. We suggest that E allows binding of SafA to a second region in SpoVID, enabling CotE to interact with E and SpoVID to function as a non-competitive hub during spore encasement.

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Citations

Dec 26, 2018·Molecular Microbiology·Bentley ShusterPatrick Eichenberger
Dec 15, 2020·PLoS Genetics·Johana LuhurChristopher D A Rodrigues

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Methods Mentioned

BETA
fluorescence microscopy
pull down
phase contrast microscopy
electron microscopy
transmission electron microscopy
phase
phage display
pulldown

Software Mentioned

SpoVID
NIS Elements AR
NIS AR
SafA
Metamorph
ImageJ 3D Surface Plot
ImageJ

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