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Co‐operation between two coiled coil cytoskeletons in polar growth in Streptomyces
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Microbiology.
Department of Biology, Lund University.
Department of Biology, Lund University.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Molecular tools.
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(English)Manuscript (preprint) (Other academic)
URN: urn:nbn:se:uu:diva-158269OAI: oai:DiVA.org:uu-158269DiVA: diva2:438905
Available from: 2011-09-06 Created: 2011-09-06 Last updated: 2011-11-03
In thesis
1. Coiled coil Cytoskeleton in Bacterial Cell Architecture: Studies of Growth and Development in Streptomyces
Open this publication in new window or tab >>Coiled coil Cytoskeleton in Bacterial Cell Architecture: Studies of Growth and Development in Streptomyces
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Bacterial cytoskeleton is an exciting and relatively new field of research. Recent findings have proven that microbes are well-organized and neatly structured organisms. In this study we have shown that intermediate filament-like proteins with a characteristic rod domain architecture of coiled coil segments separated by non-coiled coil linkers, are widely spread among bacteria.

We identified and characterized an intermediate filament-like protein (named FilP after filamentous protein) in Streptomyces coelicolor. It shares the characteristic biochemical property of eukaryotic intermediate filaments of formation of spontaneous filaments in vitro without requiring any energy or co-factor. We have provided here a preliminary model of its assembly in vitro. FilP also forms in vivo filaments in S. coelicolor hyphae, which are strongest at the sub-apical location of growing vegetative hyphae. We have proposed that FilP cytoskeletal network provides rigidity to the hyphae, especially at the growing tips, by interacting with an essential coiled coil protein DivIVA and possibly other partner elements, yet to be found.

S. coelicolor is a well-studied model organism with a complicated life cycle. It germinates from a spore and spreads by forming branched vegetative hyphae. Lack of nutrients in the environment initiates formation of aerial hyphae in the air, perpendicular to the vegetative ones. The aerial hyphae differentiate into spore chains and eventually grey-pigmented dispersed individual spores are released. The signals involved in sporulation including cell division and chromosome segregation are not clear yet. We characterized here a novel locus consisting of two genes: a small putative membrane protein with no defined function, named SmeA and a member of the SpoIIIE/FtsK family, called SffA. The expression of this locus appears to be dependent on whiA and whiG-whiH-whiI pathways. This finding is intriguing as it can provide insight to the relationship between two apparently unrelated pathways, both leading to the same function of septation and maturation during sporulation.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2011. 64 p.
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 849
Coiled coil proteins, Bacterial cytoskeleton, Differentiation
National Category
Biochemistry and Molecular Biology
urn:nbn:se:uu:diva-158271 (URN)978-91-554-8145-2 (ISBN)
Public defence
2011-10-13, B41, Husargatan 3, Bio medical Center (BMC), Uppsala, 09:15 (English)
Available from: 2011-09-22 Created: 2011-09-06 Last updated: 2011-11-03Bibliographically approved

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