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

• Type of Material: Article
• Authors: Filipa Nunes, Universidade Nova de Lisboa; Catarina Fernandes, Universidade Nova de Lisboa; Carolina Freitas, Universidade Nova de Lisboa; Eleonora Marini, Universidade Nova de Lisboa; Monica Serrano, Universidade Nova de Lisboa; Charles Moran Jr., Emory University; Patrick Eichenberger, New York University; Adriano O. Henriques, Universidade Nova de Lisboa
• Language: English
• Date: 2018-11-01
• Publisher: Wiley: 12 months
• Publication Version: Final Published Version
• Copyright Statement: © 2018 The Authors.
• License: Creative Commons Attribution 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1111/mmi.14116
• Title of Journal or Parent Work: Molecular Microbiology
• ISSN: 0950-382X
• Volume: 110
• Issue: 4
• Start Page: 576
• End Page: 595
• Grant/Funding Information: The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.; We also acknowledge the National Institute of General and Medical Sciences Public Health Services Grant GM081571 to P.E. and R01 GM110000‐04 to CPM Jr.; C.F. (SFRH/BD/43200/2008) and F.N. (SFRH/BD/64470/2009) were the recipients of doctoral fellowships from the FCT.; Part of this work was supported by funds from the Zegar Family Foundation.; This work was partially supported by Project LISBOA‐01‐0145‐FEDER‐007660 (‘Microbiologia Molecular, Estrutural e Celular’) funded by FEDER funds through COMPETE2020 – ‘Programa Operacional Competitividade e Internacionalização’ (POCI), by ONEIDA project (LISBOA‐01‐0145‐FEDER‐016417) co‐funded by FEEI ‐ "Fundos Europeus Estruturais e de Investimento" from "Programa Operacional Regional Lisboa 2020" and by national funds from FCT ‐ "Fundação para a Ciência e a Tecnologia” and through programme IF (IF/00268/2013/CP1173/CT0006) to M.S.
• Keywords: MORPHOGENETIC PROTEIN; Biochemistry & Molecular Biology; Microbiology; RECOGNITION; LOCALIZATION; Life Sciences & Biomedicine; SAFA; BACTERIAL ENDOSPORE; SPORULATION GENE; DYNAMICS; MEMBRANE; REGIONS; GERMINATION; Science & Technology
• Research Categories: Biology, Microbiology; Chemistry, Biochemistry; Biology, Molecular

Abstract

Molecular Microbiology Published by John Wiley & Sons Ltd. 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.