Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth in Streptomyces
| Autor: | Gabriella H. Kelemen, Michael D. Gillespie, Andrew M. Hemmings, Neil A. Holmes, Annabelle Thibessard, Kate A. Dalton, John Walshaw, Bertolt Gust, Richard M. Leggett |
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| Přispěvatelé: | University of East Anglia [Norwich] (UEA), John Innes Centre [Norwich], Dynamique des Génomes et Adaptation Microbienne (DynAMic), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Cell division
[SDV]Life Sciences [q-bio] Modified hendecad coiled coil Cell Cycle Proteins Streptomyces coelicolor Plasma protein binding Streptomyces Cell wall 03 medical and health sciences Bacterial Proteins Microscopy Electron Transmission Cell Wall Cell polarity Coiled coil protein Cell Cycle Protein 030304 developmental biology 0303 health sciences Multidisciplinary Microscopy Confocal biology 030306 microbiology Cell Polarity biology.organism_classification Cell biology Polar multiprotein assembly PNAS Plus Multiprotein Complexes Mutation Electrophoresis Polyacrylamide Gel Bacterial polarized growth Carrier Proteins Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (5), pp.E397-E406. ⟨10.1073/pnas.1210657110⟩ |
| ISSN: | 0027-8424 1091-6490 |
| DOI: | 10.1073/pnas.1210657110⟩ |
| Popis: | Polarized growth in eukaryotes requires polar multiprotein complexes. Here, we establish that selection and maintenance of cell polarity for growth also requires a dedicated multiprotein assembly in the filamentous bacterium, Streptomyces coelicolor . We present evidence for a tip organizing center and confirm two of its main components: Scy ( Streptomyces cytoskeletal element), a unique bacterial coiled-coil protein with an unusual repeat periodicity, and the known polarity determinant DivIVA. We also establish a link between the tip organizing center and the filament-forming protein FilP. Interestingly, both deletion and overproduction of Scy generated multiple polarity centers, suggesting a mechanism wherein Scy can both promote and limit the number of emerging polarity centers via the organization of the Scy-DivIVA assemblies. We propose that Scy is a molecular “assembler,” which, by sequestering DivIVA, promotes the establishment of new polarity centers for de novo tip formation during branching, as well as supporting polarized growth at existing hyphal tips. |
| Databáze: | OpenAIRE |
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