Disorder and amino acid composition in proteins: their potential role in the adaptation of extracellular pilins to the acidic media, where Acidithiobacillus thiooxidans grows.
Acidophiles
Biophysics
Isoelectric point
Pilins
Protein disorder
Protein stability
Journal
Extremophiles : life under extreme conditions
ISSN: 1433-4909
Titre abrégé: Extremophiles
Pays: Germany
ID NLM: 9706854
Informations de publication
Date de publication:
17 Oct 2023
17 Oct 2023
Historique:
received:
08
03
2023
accepted:
26
09
2023
medline:
23
10
2023
pubmed:
18
10
2023
entrez:
17
10
2023
Statut:
epublish
Résumé
There are few biophysical studies or structural characterizations of the type IV pilin system of extremophile bacteria, such as the acidophilic Acidithiobacillus thiooxidans. We set out to analyze their pili-comprising proteins, pilins, because these extracellular proteins are in constant interaction with protons of the acidic medium in which At. thiooxidans grows. We used the web server Operon Mapper to analyze and identify the cluster codified by the minor pilin of At. thiooxidans. In addition, we carried an in-silico characterization of such pilins using the VL-XT algorithm of PONDR® server. Our results showed that structural disorder prevails more in pilins of At. thiooxidans than in non-acidophilic bacteria. Further computational characterization showed that the pilins of At. thiooxidans are significantly enriched in hydroxy (serine and threonine) and amide (glutamine and asparagine) residues, and significantly reduced in charged residues (aspartic acid, glutamic acid, arginine and lysine). Similar results were obtained when comparing pilins from other Acidithiobacillus and other acidophilic bacteria from another genus versus neutrophilic bacteria, suggesting that these properties are intrinsic to pilins from acidic environments, most likely by maintaining solubility and stability in harsh conditions. These results give guidelines for the application of extracellular proteins of acidophiles in protein engineering.
Identifiants
pubmed: 37848738
doi: 10.1007/s00792-023-01317-z
pii: 10.1007/s00792-023-01317-z
doi:
Substances chimiques
Fimbriae Proteins
147680-16-8
Amino Acids
0
Acids
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
31Subventions
Organisme : Consejo Nacional de Ciencia y Tecnología
ID : CONACyT-CB2017-2018 Project A1-S-11505
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature Japan KK, part of Springer Nature.
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