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Apical assemblies of intermediate filament-like protein FilP are highly dynamic and affect polar growth determinant DivIVA in Streptomyces venezuelae

Fröjd, Markus J. LU and Flärdh, Klas LU (2019) In Molecular Microbiology
Abstract

Streptomyces spp. grow as branching hyphae, building the cell wall in restricted zones at hyphal tips. The organization of this mode of polar growth involves three coiled-coil proteins: DivIVA and Scy, which form apical protein complexes referred to as polarisomes; and the intermediate filament-like protein FilP, which influences cell shape and interacts with both Scy and DivIVA. Here, we use live cell imaging of Streptomyces venezuelae to clarify the subcellular localization and dynamics of FilP and its effect on hyphal morphology. By monitoring a FilP-mCherry fusion protein, we show that FilP accumulates in gradient-like zones behind the hyphal tips. The apical gradient pattern of FilP localization is dependent on hyphal tip extension... (More)

Streptomyces spp. grow as branching hyphae, building the cell wall in restricted zones at hyphal tips. The organization of this mode of polar growth involves three coiled-coil proteins: DivIVA and Scy, which form apical protein complexes referred to as polarisomes; and the intermediate filament-like protein FilP, which influences cell shape and interacts with both Scy and DivIVA. Here, we use live cell imaging of Streptomyces venezuelae to clarify the subcellular localization and dynamics of FilP and its effect on hyphal morphology. By monitoring a FilP-mCherry fusion protein, we show that FilP accumulates in gradient-like zones behind the hyphal tips. The apical gradient pattern of FilP localization is dependent on hyphal tip extension and immediately dissipates upon growth arrest. Fluorescence recovery after photobleaching experiments show that FilP gradients are dynamic and subject to subunit exchange during vegetative growth. Further, the localization of FilP at hyphal tips is not directly dependent on scy, even though the strongly perturbed morphology of most scy mutant hyphae is associated with mislocalization of FilP. Finally, we find that filP has an effect on the size and position of the foci of key polar growth determinant DivIVA. This effect likely contributes to the phenotype of filP mutants.

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Contribution to journal
publication status
epub
subject
in
Molecular Microbiology
publisher
Wiley-Blackwell
external identifiers
  • scopus:85064515325
ISSN
0950-382X
DOI
10.1111/mmi.14253
language
English
LU publication?
yes
id
60194c5a-6a6f-401c-9414-aecf221ece81
date added to LUP
2019-05-06 14:30:09
date last changed
2019-05-28 03:57:48
@article{60194c5a-6a6f-401c-9414-aecf221ece81,
  abstract     = {<p>Streptomyces spp. grow as branching hyphae, building the cell wall in restricted zones at hyphal tips. The organization of this mode of polar growth involves three coiled-coil proteins: DivIVA and Scy, which form apical protein complexes referred to as polarisomes; and the intermediate filament-like protein FilP, which influences cell shape and interacts with both Scy and DivIVA. Here, we use live cell imaging of Streptomyces venezuelae to clarify the subcellular localization and dynamics of FilP and its effect on hyphal morphology. By monitoring a FilP-mCherry fusion protein, we show that FilP accumulates in gradient-like zones behind the hyphal tips. The apical gradient pattern of FilP localization is dependent on hyphal tip extension and immediately dissipates upon growth arrest. Fluorescence recovery after photobleaching experiments show that FilP gradients are dynamic and subject to subunit exchange during vegetative growth. Further, the localization of FilP at hyphal tips is not directly dependent on scy, even though the strongly perturbed morphology of most scy mutant hyphae is associated with mislocalization of FilP. Finally, we find that filP has an effect on the size and position of the foci of key polar growth determinant DivIVA. This effect likely contributes to the phenotype of filP mutants.</p>},
  author       = {Fröjd, Markus J. and Flärdh, Klas},
  issn         = {0950-382X},
  language     = {eng},
  month        = {03},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {Apical assemblies of intermediate filament-like protein FilP are highly dynamic and affect polar growth determinant DivIVA in Streptomyces venezuelae},
  url          = {http://dx.doi.org/10.1111/mmi.14253},
  year         = {2019},
}