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Domains involved in the in vivo function and oligomerization of apical growth determinant DivIVA in Streptomyces coelicolor.

Wang, Shengbing LU ; Cantlay, Stuart LU ; Nordberg, Niklas; Letek, Michal; Gil, José A and Flärdh, Klas LU (2009) In FEMS Microbiology Letters 297. p.101-109
Abstract
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... (More)
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. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEMS Microbiology Letters
volume
297
pages
101 - 109
publisher
Elsevier
external identifiers
  • wos:000267697700015
  • scopus:67650721276
ISSN
1574-6968
DOI
10.1111/j.1574-6968.2009.01678.x
language
English
LU publication?
yes
id
e3db8246-c95d-4428-8e9c-2b36c90657f7 (old id 1433938)
date added to LUP
2009-07-02 16:07:04
date last changed
2017-08-13 03:58:15
@article{e3db8246-c95d-4428-8e9c-2b36c90657f7,
  abstract     = {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.},
  author       = {Wang, Shengbing and Cantlay, Stuart and Nordberg, Niklas and Letek, Michal and Gil, José A and Flärdh, Klas},
  issn         = {1574-6968},
  language     = {eng},
  pages        = {101--109},
  publisher    = {Elsevier},
  series       = {FEMS Microbiology Letters},
  title        = {Domains involved in the in vivo function and oligomerization of apical growth determinant DivIVA in Streptomyces coelicolor.},
  url          = {http://dx.doi.org/10.1111/j.1574-6968.2009.01678.x},
  volume       = {297},
  year         = {2009},
}