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Domains involved in the in vivo function and oligomerization of apical growth determinant DivIVA in Streptomyces coelicolor
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
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2009 (English)In: FEMS Microbiology Letters, ISSN 0378-1097, E-ISSN 1574-6968, Vol. 297, no 1, 101-109 p.Article in journal (Refereed) Published
Abstract [en]

The coiled-coil protein DivIVA is a determinant of apical growth and hyphal branching in Streptomyces coelicolor. We have investigated the properties of this protein and the involvement of different domains in its essential function and subcellular targeting. In S. coelicolor cell extracts, DivIVA was present as large oligomeric complexes that were not strongly membrane associated. The purified protein could self-assemble into extensive protein filaments in vitro. Two large and conspicuous segments in the amino acid sequence of streptomycete DivIVAs not present in other homologs, an internal PQG-rich segment and a carboxy-terminal extension, are shown to be dispensable for the essential function in S. coelicolor. Instead, the highly conserved amino-terminal of 22 amino acids was required and affected establishment of new DivIVA foci and hyphal branches, and an essential coiled-coil domain affected oligomerization of the protein.

Place, publisher, year, edition, pages
2009. Vol. 297, no 1, 101-109 p.
Keyword [en]
apical growth, cell polarity, Streptomyces, hyphae, DivIVA, coiled coil
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-128397DOI: 10.1111/j.1574-6968.2009.01678.xISI: 000267697700015OAI: oai:DiVA.org:uu-128397DiVA: diva2:331523
Available from: 2010-07-23 Created: 2010-07-20 Last updated: 2017-12-12Bibliographically approved

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