dc.contributor.author
Springstein, Benjamin L.
dc.contributor.author
Nürnberg, Dennis J.
dc.contributor.author
Woehle, Christian
dc.contributor.author
Weissenbach, Julia
dc.contributor.author
Theune, Marius L.
dc.contributor.author
Helbig, Andreas O.
dc.contributor.author
Maldener, Iris
dc.contributor.author
Dagan, Tal
dc.contributor.author
Stucken, Karina
dc.date.accessioned
2022-05-11T08:59:19Z
dc.date.available
2022-05-11T08:59:19Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/34393
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-34111
dc.description.abstract
Polymerizing and filament-forming proteins are instrumental for numerous cellular processes such as cell division and growth. Their function in stabilization and localization of protein complexes and replicons is achieved by a filamentous structure. Known filamentous proteins assemble into homopolymers consisting of single subunits – for example, MreB and FtsZ in bacteria – or heteropolymers that are composed of two subunits, for example, keratin and α/β tubulin in eukaryotes. Here, we describe two novel coiled-coil-rich proteins (CCRPs) in the filament-forming cyanobacterium Anabaena sp. PCC 7120 (hereafter Anabaena) that assemble into a heteropolymer and function in the maintenance of the Anabaena multicellular shape (termed trichome). The two CCRPs – Alr4504 and Alr4505 (named ZicK and ZacK) – are strictly interdependent for the assembly of protein filaments in vivo and polymerize nucleotide independently in vitro, similar to known intermediate filament (IF) proteins. A ΔzicKΔzacK double mutant is characterized by a zigzagged cell arrangement and hence a loss of the typical linear Anabaena trichome shape. ZicK and ZacK interact with themselves, with each other, with the elongasome protein MreB, the septal junction protein SepJ and the divisome associate septal protein SepI. Our results suggest that ZicK and ZacK function in cooperation with SepJ and MreB to stabilize the Anabaena trichome and are likely essential for the manifestation of the multicellular shape in Anabaena. Our study reveals the presence of filament-forming IF-like proteins whose function is achieved through the formation of heteropolymers in cyanobacteria.
en
dc.format.extent
20 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
cyanobacteria
en
dc.subject
heteropolymer
en
dc.subject
multicellular shape
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik::539 Moderne Physik
dc.title
Two novel heteropolymer‐forming proteins maintain the multicellular shape of the cyanobacterium Anabaena sp. PCC 7120
dc.type
Wissenschaftlicher Artikel
dc.identifier.sepid
86660
dcterms.bibliographicCitation.doi
10.1111/febs.15630
dcterms.bibliographicCitation.journaltitle
The FEBS Journal
dcterms.bibliographicCitation.number
10
dcterms.bibliographicCitation.originalpublishername
Wiley-Blackwell
dcterms.bibliographicCitation.originalpublisherplace
Oxford
dcterms.bibliographicCitation.pagestart
3197
dcterms.bibliographicCitation.pageend
3216
dcterms.bibliographicCitation.volume
288 (2021)
dcterms.bibliographicCitation.url
https://onlinelibrary.wiley.com/doi/10.1111/febs.15630
refubium.affiliation
Physik
refubium.affiliation.other
Institut für Experimentalphysik
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refubium.note.author
korr., erg., OA, 11.05.22 Siev
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
1742-464X
dcterms.isPartOf.eissn
1742-4658