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A dispensable SepIVA orthologue in Streptomyces venezuelae is associated with polar growth and not cell division

Sen, Beer Chakra LU ; Mavi, Parminder Singh LU ; Irazoki, Oihane ; Datta, Susmita ; Kaiser, Sebastian ; Cava, Felipe and Flärdh, Klas LU (2024) In BMC Microbiology 24(1).
Abstract

Background: SepIVA has been reported to be an essential septation factor in Mycolicibacterium smegmatis and Mycobacterium tuberculosis. It is a coiled-coil protein with similarity to DivIVA, a protein necessary for polar growth in members of the phylum Actinomycetota. Orthologues of SepIVA are broadly distributed among actinomycetes, including in Streptomyces spp. Results: To clarify the role of SepIVA and its potential involvement in cell division in streptomycetes, we generated sepIVA deletion mutants in Streptomyces venezuelae and found that sepIVA is dispensable for growth, cell division and sporulation. Further, mNeonGreen-SepIVA fusion protein did not localize at division septa, and we found no evidence of involvement of SepIVA in... (More)

Background: SepIVA has been reported to be an essential septation factor in Mycolicibacterium smegmatis and Mycobacterium tuberculosis. It is a coiled-coil protein with similarity to DivIVA, a protein necessary for polar growth in members of the phylum Actinomycetota. Orthologues of SepIVA are broadly distributed among actinomycetes, including in Streptomyces spp. Results: To clarify the role of SepIVA and its potential involvement in cell division in streptomycetes, we generated sepIVA deletion mutants in Streptomyces venezuelae and found that sepIVA is dispensable for growth, cell division and sporulation. Further, mNeonGreen-SepIVA fusion protein did not localize at division septa, and we found no evidence of involvement of SepIVA in cell division. Instead, mNeonGreen-SepIVA was accumulated at the tips of growing vegetative hyphae in ways reminiscent of the apical localization of polarisome components like DivIVA. Bacterial two-hybrid system analyses revealed an interaction between SepIVA and DivIVA. The results indicate that SepIVA is associated with polar growth. However, no phenotypic effects of sepIVA deletion could be detected, and no evidence was observed of redundancy with the other DivIVA-like coiled-coil proteins Scy and FilP that are also associated with apical growth in streptomycetes. Conclusions: We conclude that S. venezuelae SepIVA, in contrast to the situation in mycobacteria, is dispensable for growth and viability. The results suggest that it is associated with polar growth rather than septum formation.

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Cell division, Cell wall synthesis, FtsZ, Polar growth, Streptomyces
in
BMC Microbiology
volume
24
issue
1
article number
481
publisher
BioMed Central (BMC)
external identifiers
  • scopus:85209567520
  • pmid:39558276
ISSN
1471-2180
DOI
10.1186/s12866-024-03625-6
language
English
LU publication?
yes
id
495321d4-411e-4d4c-b33f-fb08e39b9a54
date added to LUP
2025-01-15 10:55:08
date last changed
2025-07-17 01:54:25
@article{495321d4-411e-4d4c-b33f-fb08e39b9a54,
  abstract     = {{<p>Background: SepIVA has been reported to be an essential septation factor in Mycolicibacterium smegmatis and Mycobacterium tuberculosis. It is a coiled-coil protein with similarity to DivIVA, a protein necessary for polar growth in members of the phylum Actinomycetota. Orthologues of SepIVA are broadly distributed among actinomycetes, including in Streptomyces spp. Results: To clarify the role of SepIVA and its potential involvement in cell division in streptomycetes, we generated sepIVA deletion mutants in Streptomyces venezuelae and found that sepIVA is dispensable for growth, cell division and sporulation. Further, mNeonGreen-SepIVA fusion protein did not localize at division septa, and we found no evidence of involvement of SepIVA in cell division. Instead, mNeonGreen-SepIVA was accumulated at the tips of growing vegetative hyphae in ways reminiscent of the apical localization of polarisome components like DivIVA. Bacterial two-hybrid system analyses revealed an interaction between SepIVA and DivIVA. The results indicate that SepIVA is associated with polar growth. However, no phenotypic effects of sepIVA deletion could be detected, and no evidence was observed of redundancy with the other DivIVA-like coiled-coil proteins Scy and FilP that are also associated with apical growth in streptomycetes. Conclusions: We conclude that S. venezuelae SepIVA, in contrast to the situation in mycobacteria, is dispensable for growth and viability. The results suggest that it is associated with polar growth rather than septum formation.</p>}},
  author       = {{Sen, Beer Chakra and Mavi, Parminder Singh and Irazoki, Oihane and Datta, Susmita and Kaiser, Sebastian and Cava, Felipe and Flärdh, Klas}},
  issn         = {{1471-2180}},
  keywords     = {{Cell division; Cell wall synthesis; FtsZ; Polar growth; Streptomyces}},
  language     = {{eng}},
  number       = {{1}},
  publisher    = {{BioMed Central (BMC)}},
  series       = {{BMC Microbiology}},
  title        = {{A dispensable SepIVA orthologue in Streptomyces venezuelae is associated with polar growth and not cell division}},
  url          = {{http://dx.doi.org/10.1186/s12866-024-03625-6}},
  doi          = {{10.1186/s12866-024-03625-6}},
  volume       = {{24}},
  year         = {{2024}},
}