A histidine pseudokinase modulates polar growth and cell shape in Streptomyces venezuelae
(2026) In Communications Biology 9(1).- Abstract
Polar growth and cell shape determination in mycelium-forming Streptomyces bacteria depends on the function of a polarly localised multiprotein complex that directs cell wall synthesis – the polarisome. This complex assembles around the essential cell polarity determinant DivIVA, alongside other largely unknown components. We report here the discovery of a conserved hybrid histidine kinase-like protein, PsmA, that interacts and co-localises with DivIVA at the hyphal tips. Deletion of psmA affects the shape and dynamics of the polarisome, leading to aberrant cell shape and hyphal hyperbranching. PsmA is a pseudokinase that lacks the critical histidine residue in its catalytic core. Our results suggest that PsmA tunes the dynamics and... (More)
Polar growth and cell shape determination in mycelium-forming Streptomyces bacteria depends on the function of a polarly localised multiprotein complex that directs cell wall synthesis – the polarisome. This complex assembles around the essential cell polarity determinant DivIVA, alongside other largely unknown components. We report here the discovery of a conserved hybrid histidine kinase-like protein, PsmA, that interacts and co-localises with DivIVA at the hyphal tips. Deletion of psmA affects the shape and dynamics of the polarisome, leading to aberrant cell shape and hyphal hyperbranching. PsmA is a pseudokinase that lacks the critical histidine residue in its catalytic core. Our results suggest that PsmA tunes the dynamics and properties of the DivIVA-based polar organelle in streptomycetes in parallel to but not redundantly with Scy and FilP, two coiled-coil proteins known to influence polarisome properties. In summary, PsmA interacts with DivIVA and modulates the integrity of the growth zones at hyphal tips.
(Less)
- author
- Singh Mavi, Parminder LU and Flärdh, Klas LU
- organization
- publishing date
- 2026
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Communications Biology
- volume
- 9
- issue
- 1
- article number
- 345
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:105032234460
- pmid:41620559
- ISSN
- 2399-3642
- DOI
- 10.1038/s42003-026-09620-z
- language
- English
- LU publication?
- yes
- id
- b541e340-2f93-44dd-9060-66a459a4b37d
- date added to LUP
- 2026-04-23 12:53:04
- date last changed
- 2026-06-04 15:37:48
@article{b541e340-2f93-44dd-9060-66a459a4b37d,
abstract = {{<p>Polar growth and cell shape determination in mycelium-forming Streptomyces bacteria depends on the function of a polarly localised multiprotein complex that directs cell wall synthesis – the polarisome. This complex assembles around the essential cell polarity determinant DivIVA, alongside other largely unknown components. We report here the discovery of a conserved hybrid histidine kinase-like protein, PsmA, that interacts and co-localises with DivIVA at the hyphal tips. Deletion of psmA affects the shape and dynamics of the polarisome, leading to aberrant cell shape and hyphal hyperbranching. PsmA is a pseudokinase that lacks the critical histidine residue in its catalytic core. Our results suggest that PsmA tunes the dynamics and properties of the DivIVA-based polar organelle in streptomycetes in parallel to but not redundantly with Scy and FilP, two coiled-coil proteins known to influence polarisome properties. In summary, PsmA interacts with DivIVA and modulates the integrity of the growth zones at hyphal tips.</p>}},
author = {{Singh Mavi, Parminder and Flärdh, Klas}},
issn = {{2399-3642}},
language = {{eng}},
number = {{1}},
publisher = {{Nature Publishing Group}},
series = {{Communications Biology}},
title = {{A histidine pseudokinase modulates polar growth and cell shape in Streptomyces venezuelae}},
url = {{http://dx.doi.org/10.1038/s42003-026-09620-z}},
doi = {{10.1038/s42003-026-09620-z}},
volume = {{9}},
year = {{2026}},
}