The Thioredoxin Fold Protein (TFP2) from Extreme Acidophilic <i>Leptospirillum</i> sp. CF-1 Is a Chaperedoxin-like Protein That Prevents the Aggregation of Proteins under Oxidative Stress

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dc.contributor.authorMunoz-Villagran, Claudia
dc.contributor.authorAcevedo-Arbunic, Javiera
dc.contributor.authorHaertig, Elisabeth
dc.contributor.authorIssotta, Francisco
dc.contributor.authorMascayano, Carolina
dc.contributor.authorJahn, Dieter
dc.contributor.authorJahn, Martina
dc.contributor.authorLevican, Gloria
dc.date.accessioned2025-01-20T16:13:01Z
dc.date.available2025-01-20T16:13:01Z
dc.date.issued2024
dc.description.abstractExtreme acidophilic bacteria like Leptospirillum sp. require an efficient enzyme system to counteract strong oxygen stress conditions in their natural habitat. The genome of Leptospirillum sp. CF-1 encodes the thioredoxin-fold protein TFP2, which exhibits a high structural similarity to the thioredoxin domain of E. coli CnoX. CnoX from Escherichia coli is a chaperedoxin that protects protein substrates from oxidative stress conditions using its holdase function and a subsequent transfer to foldase chaperones for refolding. Recombinantly produced and purified Leptospirillum sp. TFP2 possesses both thioredoxin and chaperone holdase activities in vitro. It can be reduced by thioredoxin reductase (TrxR). The tfp2 gene co-locates with genes for the chaperone foldase GroES/EL on the chromosome. The "tfp2 cluster" (ctpA-groES-groEL-hyp-tfp2-recN) was found between 1.9 and 8.8-fold transcriptionally up-regulated in response to 1 mM hydrogen peroxide (H2O2). Leptospirillum sp. tfp2 heterologously expressed in E. coli wild type and cnoX mutant strains lead to an increased tolerance of these E. coli strains to H2O2 and significantly reduced intracellular protein aggregates. Finally, a proteomic analysis of protein aggregates produced in E. coli upon exposition to oxidative stress with 4 mM H2O2, showed that Leptospirillum sp. tfp2 expression caused a significant decrease in the aggregation of 124 proteins belonging to fifteen different metabolic categories. These included several known substrates of DnaK and GroEL/ES. These findings demonstrate that Leptospirillum sp. TFP2 is a chaperedoxin-like protein, acting as a key player in the control of cellular proteostasis under highly oxidative conditions that prevail in extreme acidic environments.
dc.fuente.origenWOS
dc.identifier.doi10.3390/ijms25136905
dc.identifier.eissn1422-0067
dc.identifier.issn1661-6596
dc.identifier.urihttps://doi.org/10.3390/ijms25136905
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/90368
dc.identifier.wosidWOS:001270261400001
dc.issue.numero13
dc.language.isoen
dc.revistaInternational journal of molecular sciences
dc.rightsacceso restringido
dc.subjectacidophiles
dc.subjectchaperedoxin
dc.subjectCnoX
dc.subjectLeptospirillum
dc.subjectTFP2
dc.subjectthioredoxin
dc.subjectprotein aggregation
dc.subjectproteostasis
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleThe Thioredoxin Fold Protein (TFP2) from Extreme Acidophilic <i>Leptospirillum</i> sp. CF-1 Is a Chaperedoxin-like Protein That Prevents the Aggregation of Proteins under Oxidative Stress
dc.typeartículo
dc.volumen25
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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