Two novel heteropolymer-forming proteins maintain the multicellular shape of the cyanobacterium Anabaena sp. PCC 7120.


Journal

The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646

Informations de publication

Date de publication:
05 2021
Historique:
revised: 29 10 2020
received: 09 06 2020
accepted: 13 11 2020
pubmed: 19 11 2020
medline: 22 7 2021
entrez: 18 11 2020
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 33205554
doi: 10.1111/febs.15630
doi:

Substances chimiques

Bacterial Proteins 0
Cytoskeletal Proteins 0
His-His-His-His-His-His 0
Oligopeptides 0
Recombinant Fusion Proteins 0
enhanced cyan fluorescent protein 0
Green Fluorescent Proteins 147336-22-9
Histidine 4QD397987E

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

3197-3216

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L011506/1
Pays : United Kingdom

Informations de copyright

© 2020 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

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Auteurs

Benjamin L Springstein (BL)

Institute of General Microbiology, University of Kiel, Germany.

Dennis J Nürnberg (DJ)

Department of Life Sciences, Imperial College, London, UK.

Christian Woehle (C)

Institute of General Microbiology, University of Kiel, Germany.

Julia Weissenbach (J)

Institute of General Microbiology, University of Kiel, Germany.

Marius L Theune (ML)

Institute of General Microbiology, University of Kiel, Germany.

Andreas O Helbig (AO)

AG Proteomics & Bioanalytics, Institute for Experimental Medicine, Christian-Albrechts-Universität zu Kiel, Germany.

Iris Maldener (I)

Interfaculty Institute of Microbiology and Infection Medicine Tübingen/Organismic Interactions, University of Tübingen, Germany.

Tal Dagan (T)

Institute of General Microbiology, University of Kiel, Germany.

Karina Stucken (K)

Department of Food Engineering, University of La Serena, Chile.

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