The HlyD-like membrane fusion protein All5304 is essential for acid stress survival of the filamentous cyanobacterium Anabaena sp. PCC 7120.
Anabaena sp. PCC 7120
acid stress
cyanobacterium
membrane fusion protein
tripartite efflux pump
type I secretion system
Journal
FEMS microbiology letters
ISSN: 1574-6968
Titre abrégé: FEMS Microbiol Lett
Pays: England
ID NLM: 7705721
Informations de publication
Date de publication:
01 08 2020
01 08 2020
Historique:
received:
03
03
2020
accepted:
25
06
2020
pubmed:
28
6
2020
medline:
14
7
2021
entrez:
28
6
2020
Statut:
ppublish
Résumé
Acid stress is an environmental problem for plants and fresh water cyanobacteria like the filamentous, heterocyst forming species Anabaena sp. PCC 7120 (hereafter Anabaena sp.). Heterocyst differentiation, cell-cell communication and nitrogen fixation has been deeply studied in this model organism, but little is known about the cellular response of Anabaena sp. to decreased pH values, causing acid stress. ATP-binding cassette (ABC) transporters are involved in acid stress response in other bacteria, by exporting proteins responsible for survival under acidification. The genome of Anabaena sp. encodes numerous ABC transporter components, whose function is not known yet. Here, we describe the function of the gene all5304 encoding a protein with homology to membrane fusion proteins of tripartite efflux pumps driven by ABC transporters like HlyBD-TolC of Escherichia coli. The all5304 mutant shows less resistance against low pH, even though the expression of the gene is independent from the pH of the medium. We compared the exoproteome of the wild type and mutant cultures and identified three proteins-candidate substrates of the putative transporter. Including the in silico analysis of All5304, our results suggest that All5304 functions as part of an efflux pump, secreting of a protein necessary for acid tolerance in Anabaena sp.
Identifiants
pubmed: 32592389
pii: 5863934
doi: 10.1093/femsle/fnaa108
pii:
doi:
Substances chimiques
Acids
0
Hemolysin Proteins
0
Membrane Fusion Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© FEMS 2020.