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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ftunivnapoliiris:oai:www.iris.unina.it:11588/447670 2024-09-09T19:09:06+00:00 Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 Falasca P. Evangelista G. COTUGNO, ROBERTA MARCO, SALVATORE MASULLO, MARIOROSARIO DE VENDITTIS, EMMANUELE RAIMO, GENNARO Falasca, P. Evangelista, G. Cotugno, Roberta Marco, Salvatore Masullo, Mariorosario DE VENDITTIS, Emmanuele Raimo, Gennaro 2012 http://hdl.handle.net/11588/447670 https://doi.org/10.1007/s00792-012-0453-0 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000303870300019 volume:16 firstpage:539 lastpage:552 numberofpages:14 journal:EXTREMOPHILES http://hdl.handle.net/11588/447670 doi:10.1007/s00792-012-0453-0 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84860841914 Thioredoxin system Psychrophile Pseudoalteromonas haloplankti Temperature adaptation S-glutathionylation Energetic parameters info:eu-repo/semantics/article 2012 ftunivnapoliiris https://doi.org/10.1007/s00792-012-0453-0 2024-06-17T15:19:27Z 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 were 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 oxidized or nitrosylated forms. A mutagenic analysis realised on three non catalytic cysteines of the flavoenzyme allowed the identification of C303 as the target for the S-glutathionylation reaction. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic The Antarctic Tac ENVELOPE(-59.517,-59.517,-62.500,-62.500) Extremophiles 16 3 539 552 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
Thioredoxin system Psychrophile Pseudoalteromonas haloplankti Temperature adaptation S-glutathionylation Energetic parameters |
spellingShingle |
Thioredoxin system Psychrophile Pseudoalteromonas haloplankti Temperature adaptation S-glutathionylation Energetic parameters Falasca P. Evangelista G. COTUGNO, ROBERTA MARCO, SALVATORE MASULLO, MARIOROSARIO DE VENDITTIS, EMMANUELE RAIMO, GENNARO Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
topic_facet |
Thioredoxin system Psychrophile Pseudoalteromonas haloplankti Temperature adaptation S-glutathionylation Energetic parameters |
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 were 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 oxidized or nitrosylated forms. A mutagenic analysis realised on three non catalytic cysteines of the flavoenzyme allowed the identification of C303 as the target for the S-glutathionylation reaction. |
author2 |
Falasca, P. Evangelista, G. Cotugno, Roberta Marco, Salvatore Masullo, Mariorosario DE VENDITTIS, Emmanuele Raimo, Gennaro |
format |
Article in Journal/Newspaper |
author |
Falasca P. Evangelista G. COTUGNO, ROBERTA MARCO, SALVATORE MASULLO, MARIOROSARIO DE VENDITTIS, EMMANUELE RAIMO, GENNARO |
author_facet |
Falasca P. Evangelista G. COTUGNO, ROBERTA MARCO, SALVATORE MASULLO, MARIOROSARIO DE VENDITTIS, EMMANUELE RAIMO, GENNARO |
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/11588/447670 https://doi.org/10.1007/s00792-012-0453-0 |
long_lat |
ENVELOPE(-59.517,-59.517,-62.500,-62.500) |
geographic |
Antarctic The Antarctic Tac |
geographic_facet |
Antarctic The Antarctic Tac |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000303870300019 volume:16 firstpage:539 lastpage:552 numberofpages:14 journal:EXTREMOPHILES http://hdl.handle.net/11588/447670 doi:10.1007/s00792-012-0453-0 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84860841914 |
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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1809823377757569024 |