Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125
The endogenous components of the thioredoxin system in the Antarctic eubacterium Pseudoalteromonas haloplanktis have been purified and characterised. The temperature dependence of the activities sustained by thioredoxin (PhTrx) and thioredoxin reductase (PhTrxR) pointed to their adaptation in the co...
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Online Access: | http://hdl.handle.net/11367/23974 https://doi.org/10.1007/s00792-012-0453-0 |
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ftuninapoliparth:oai:ricerca.uniparthenope.it:11367/23974 2024-04-14T08:03:06+00:00 Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 Falasca P Evangelista G Cotugno R Marco S De Vendittis E Raimo G. MASULLO, Mariorosario Falasca, P Evangelista, G Cotugno, R Marco, S Masullo, Mariorosario De Vendittis, E Raimo, G. 2012 http://hdl.handle.net/11367/23974 https://doi.org/10.1007/s00792-012-0453-0 eng eng info:eu-repo/semantics/altIdentifier/pmid/22527046 info:eu-repo/semantics/altIdentifier/wos/WOS:000303870300019 volume:16 issue:3 firstpage:539 lastpage:552 numberofpages:14 journal:EXTREMOPHILES http://hdl.handle.net/11367/23974 doi:10.1007/s00792-012-0453-0 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84860841914 info:eu-repo/semantics/closedAccess Thioredoxin system Pseudoalteromonas haloplankti Psychrophilic info:eu-repo/semantics/article 2012 ftuninapoliparth https://doi.org/10.1007/s00792-012-0453-0 2024-03-21T18:04:13Z The endogenous components of the thioredoxin system in the Antarctic eubacterium Pseudoalteromonas haloplanktis have been purified and characterised. The temperature dependence of the activities sustained by thioredoxin (PhTrx) and thioredoxin reductase (PhTrxR) pointed to their adaptation in the cold growth environment. PhTrxR was purified as a flavoenzyme and its activity was significantly enhanced in the presence of molar concentration of monovalent cations. The energetics of the partial reactions leading to the whole electron transfer from NADPH to the target protein substrate in the reconstituted thioredoxin system was also investigated. While the initial electron transfer from NADPH to PhTrxR was energetically favoured, the final passage to the heterologous protein substrate enhanced the energetic barrier of the whole process. The energy of activation of the heat inactivation process essentially reflected the psychrophilic origin of PhTrxR. Vice versa, PhTrx possessed an exceptional heat resistance (half-life, 4.4 h at 95 °C), ranking this protein among the most thermostable enzymes reported so far in psychrophiles. PhTrxR was covalently modified by glutathione, mainly by its oxidised or nitrosylated forms. A mutagenic analysis realised on three non catalytic cysteines of the flavoenzyme allowed the identification of C(303) as the target for the S-glutathionylation reaction. Article in Journal/Newspaper Antarc* Antarctic Università degli Studi di Napoli "Parthenope": CINECA IRIS Antarctic Tac ENVELOPE(-59.517,-59.517,-62.500,-62.500) The Antarctic Extremophiles 16 3 539 552 |
institution |
Open Polar |
collection |
Università degli Studi di Napoli "Parthenope": CINECA IRIS |
op_collection_id |
ftuninapoliparth |
language |
English |
topic |
Thioredoxin system Pseudoalteromonas haloplankti Psychrophilic |
spellingShingle |
Thioredoxin system Pseudoalteromonas haloplankti Psychrophilic Falasca P Evangelista G Cotugno R Marco S De Vendittis E Raimo G. MASULLO, Mariorosario Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
topic_facet |
Thioredoxin system Pseudoalteromonas haloplankti Psychrophilic |
description |
The endogenous components of the thioredoxin system in the Antarctic eubacterium Pseudoalteromonas haloplanktis have been purified and characterised. The temperature dependence of the activities sustained by thioredoxin (PhTrx) and thioredoxin reductase (PhTrxR) pointed to their adaptation in the cold growth environment. PhTrxR was purified as a flavoenzyme and its activity was significantly enhanced in the presence of molar concentration of monovalent cations. The energetics of the partial reactions leading to the whole electron transfer from NADPH to the target protein substrate in the reconstituted thioredoxin system was also investigated. While the initial electron transfer from NADPH to PhTrxR was energetically favoured, the final passage to the heterologous protein substrate enhanced the energetic barrier of the whole process. The energy of activation of the heat inactivation process essentially reflected the psychrophilic origin of PhTrxR. Vice versa, PhTrx possessed an exceptional heat resistance (half-life, 4.4 h at 95 °C), ranking this protein among the most thermostable enzymes reported so far in psychrophiles. PhTrxR was covalently modified by glutathione, mainly by its oxidised or nitrosylated forms. A mutagenic analysis realised on three non catalytic cysteines of the flavoenzyme allowed the identification of C(303) as the target for the S-glutathionylation reaction. |
author2 |
Falasca, P Evangelista, G Cotugno, R Marco, S Masullo, Mariorosario De Vendittis, E Raimo, G. |
format |
Article in Journal/Newspaper |
author |
Falasca P Evangelista G Cotugno R Marco S De Vendittis E Raimo G. MASULLO, Mariorosario |
author_facet |
Falasca P Evangelista G Cotugno R Marco S De Vendittis E Raimo G. MASULLO, Mariorosario |
author_sort |
Falasca P |
title |
Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_short |
Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_full |
Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_fullStr |
Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_full_unstemmed |
Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_sort |
properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium pseudoalteromonas haloplanktis tac 125 |
publishDate |
2012 |
url |
http://hdl.handle.net/11367/23974 https://doi.org/10.1007/s00792-012-0453-0 |
long_lat |
ENVELOPE(-59.517,-59.517,-62.500,-62.500) |
geographic |
Antarctic Tac The Antarctic |
geographic_facet |
Antarctic Tac The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/22527046 info:eu-repo/semantics/altIdentifier/wos/WOS:000303870300019 volume:16 issue:3 firstpage:539 lastpage:552 numberofpages:14 journal:EXTREMOPHILES http://hdl.handle.net/11367/23974 doi:10.1007/s00792-012-0453-0 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84860841914 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1007/s00792-012-0453-0 |
container_title |
Extremophiles |
container_volume |
16 |
container_issue |
3 |
container_start_page |
539 |
op_container_end_page |
552 |
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1796298377673048064 |