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The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces.

Hempel, Antje; Cantlay, Stuart LU ; Molle, Virginie; Wang, Jian-Sheng; Naldrett, Mike J; Parker, Jennifer L; Richards, David M; Jung, Yong-Gyun; Buttner, Mark J and Flärdh, Klas LU (2012) In Proceedings of the National Academy of Sciences 109(35). p.2371-2379
Abstract
In cells that exhibit apical growth, mechanisms that regulate cell polarity are crucial for determination of cellular shape and for the adaptation of growth to intrinsic and extrinsic cues. Broadly conserved pathways control cell polarity in eukaryotes, but less is known about polarly growing prokaryotes. An evolutionarily ancient form of apical growth is found in the filamentous bacteria Streptomyces, and is directed by a polarisome-like complex involving the essential protein DivIVA. We report here that this bacterial polarization machinery is regulated by a eukaryotic-type Ser/Thr protein kinase, AfsK, which localizes to hyphal tips and phosphorylates DivIVA. During normal growth, AfsK regulates hyphal branching by modulating... (More)
In cells that exhibit apical growth, mechanisms that regulate cell polarity are crucial for determination of cellular shape and for the adaptation of growth to intrinsic and extrinsic cues. Broadly conserved pathways control cell polarity in eukaryotes, but less is known about polarly growing prokaryotes. An evolutionarily ancient form of apical growth is found in the filamentous bacteria Streptomyces, and is directed by a polarisome-like complex involving the essential protein DivIVA. We report here that this bacterial polarization machinery is regulated by a eukaryotic-type Ser/Thr protein kinase, AfsK, which localizes to hyphal tips and phosphorylates DivIVA. During normal growth, AfsK regulates hyphal branching by modulating branch-site selection and some aspect of the underlying polarisome-splitting mechanism that controls branching of Streptomyces hyphae. Further, AfsK is activated by signals generated by the arrest of cell wall synthesis and directly communicates this to the polarisome by hyperphosphorylating DivIVA. Induction of high levels of DivIVA phosphorylation by using a constitutively active mutant AfsK causes disassembly of apical polarisomes, followed by establishment of multiple hyphal branches elsewhere in the cell, revealing a profound impact of this kinase on growth polarity. The function of AfsK is reminiscent of the phoshorylation of polarity proteins and polarisome components by Ser/Thr protein kinases in eukaryotes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
hyphal growth, protein phosphorylation, peptidoglycan, cytoskeleton, tip extension
in
Proceedings of the National Academy of Sciences
volume
109
issue
35
pages
2371 - 2379
publisher
National Acad Sciences
external identifiers
  • wos:000308565300010
  • pmid:22869733
  • scopus:84865562049
ISSN
1091-6490
DOI
10.1073/pnas.1207409109
language
English
LU publication?
yes
id
d0aa5717-28dd-438d-bda6-1c8c6569d89f (old id 3047739)
date added to LUP
2012-09-06 13:52:28
date last changed
2017-10-22 03:18:51
@article{d0aa5717-28dd-438d-bda6-1c8c6569d89f,
  abstract     = {In cells that exhibit apical growth, mechanisms that regulate cell polarity are crucial for determination of cellular shape and for the adaptation of growth to intrinsic and extrinsic cues. Broadly conserved pathways control cell polarity in eukaryotes, but less is known about polarly growing prokaryotes. An evolutionarily ancient form of apical growth is found in the filamentous bacteria Streptomyces, and is directed by a polarisome-like complex involving the essential protein DivIVA. We report here that this bacterial polarization machinery is regulated by a eukaryotic-type Ser/Thr protein kinase, AfsK, which localizes to hyphal tips and phosphorylates DivIVA. During normal growth, AfsK regulates hyphal branching by modulating branch-site selection and some aspect of the underlying polarisome-splitting mechanism that controls branching of Streptomyces hyphae. Further, AfsK is activated by signals generated by the arrest of cell wall synthesis and directly communicates this to the polarisome by hyperphosphorylating DivIVA. Induction of high levels of DivIVA phosphorylation by using a constitutively active mutant AfsK causes disassembly of apical polarisomes, followed by establishment of multiple hyphal branches elsewhere in the cell, revealing a profound impact of this kinase on growth polarity. The function of AfsK is reminiscent of the phoshorylation of polarity proteins and polarisome components by Ser/Thr protein kinases in eukaryotes.},
  author       = {Hempel, Antje and Cantlay, Stuart and Molle, Virginie and Wang, Jian-Sheng and Naldrett, Mike J and Parker, Jennifer L and Richards, David M and Jung, Yong-Gyun and Buttner, Mark J and Flärdh, Klas},
  issn         = {1091-6490},
  keyword      = {hyphal growth,protein phosphorylation,peptidoglycan,cytoskeleton,tip extension},
  language     = {eng},
  number       = {35},
  pages        = {2371--2379},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces.},
  url          = {http://dx.doi.org/10.1073/pnas.1207409109},
  volume       = {109},
  year         = {2012},
}