Cargando…

A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus

In this study, we gain insight into the extracellular proteolytic system of Sulfolobus solfataricus grown on proteinaceous substrates, providing further evidence that acidic proteases were specifically produced in response to peptide-rich media. The main proteolytic component was the previously isol...

Descripción completa

Detalles Bibliográficos
Autores principales: Gogliettino, Marta, Riccio, Alessia, Cocca, Ennio, Rossi, Mosè, Palmieri, Gianna, Balestrieri, Marco
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3958906/
https://www.ncbi.nlm.nih.gov/pubmed/24566144
http://dx.doi.org/10.3390/ijms15023204
_version_ 1782307968337838080
author Gogliettino, Marta
Riccio, Alessia
Cocca, Ennio
Rossi, Mosè
Palmieri, Gianna
Balestrieri, Marco
author_facet Gogliettino, Marta
Riccio, Alessia
Cocca, Ennio
Rossi, Mosè
Palmieri, Gianna
Balestrieri, Marco
author_sort Gogliettino, Marta
collection PubMed
description In this study, we gain insight into the extracellular proteolytic system of Sulfolobus solfataricus grown on proteinaceous substrates, providing further evidence that acidic proteases were specifically produced in response to peptide-rich media. The main proteolytic component was the previously isolated SsMTP (Sulfolobus solfataricus multi-domain thermopsin-like protease), while the less abundant (named SsMTP-1) one was purified, characterized and identified as the sso1175 gene-product. The protein revealed a multi-domain organization shared with the cognate SsMTP with a catalytic domain followed by several tandemly-repeated motifs. Moreover, both enzymes were found spread across the Crenarchaeota phylum and belonging to the thermopsin family, although segregated into diverse phylogenetic clusters. SsMTP-1 showed a 75-kDa molecular mass and was stable in the temperature range 50–90 °C, with optimal activity at 70 °C and pH 2.0. Serine, metallo and aspartic protease inhibitors did not affect the enzyme activity, designating SsMTP-1 as a new member of the pepstatin-insensitive aspartic protease family. The peptide-bond-specificity of SsMTP-1 in the cleavage of the oxidized insulin B chain was uncommon amongst thermopsins, suggesting that it could play a distinct, but cooperative role in the protein degradation machinery. Interestingly, predictions of the transmembrane protein topology of SsMTP and SsMTP-1 strongly suggest a possible contribution in signal-transduction pathways.
format Online
Article
Text
id pubmed-3958906
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Molecular Diversity Preservation International (MDPI)
record_format MEDLINE/PubMed
spelling pubmed-39589062014-03-20 A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus Gogliettino, Marta Riccio, Alessia Cocca, Ennio Rossi, Mosè Palmieri, Gianna Balestrieri, Marco Int J Mol Sci Article In this study, we gain insight into the extracellular proteolytic system of Sulfolobus solfataricus grown on proteinaceous substrates, providing further evidence that acidic proteases were specifically produced in response to peptide-rich media. The main proteolytic component was the previously isolated SsMTP (Sulfolobus solfataricus multi-domain thermopsin-like protease), while the less abundant (named SsMTP-1) one was purified, characterized and identified as the sso1175 gene-product. The protein revealed a multi-domain organization shared with the cognate SsMTP with a catalytic domain followed by several tandemly-repeated motifs. Moreover, both enzymes were found spread across the Crenarchaeota phylum and belonging to the thermopsin family, although segregated into diverse phylogenetic clusters. SsMTP-1 showed a 75-kDa molecular mass and was stable in the temperature range 50–90 °C, with optimal activity at 70 °C and pH 2.0. Serine, metallo and aspartic protease inhibitors did not affect the enzyme activity, designating SsMTP-1 as a new member of the pepstatin-insensitive aspartic protease family. The peptide-bond-specificity of SsMTP-1 in the cleavage of the oxidized insulin B chain was uncommon amongst thermopsins, suggesting that it could play a distinct, but cooperative role in the protein degradation machinery. Interestingly, predictions of the transmembrane protein topology of SsMTP and SsMTP-1 strongly suggest a possible contribution in signal-transduction pathways. Molecular Diversity Preservation International (MDPI) 2014-02-21 /pmc/articles/PMC3958906/ /pubmed/24566144 http://dx.doi.org/10.3390/ijms15023204 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Gogliettino, Marta
Riccio, Alessia
Cocca, Ennio
Rossi, Mosè
Palmieri, Gianna
Balestrieri, Marco
A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus
title A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus
title_full A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus
title_fullStr A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus
title_full_unstemmed A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus
title_short A New Pepstatin-Insensitive Thermopsin-Like Protease Overproduced in Peptide-Rich Cultures of Sulfolobus solfataricus
title_sort new pepstatin-insensitive thermopsin-like protease overproduced in peptide-rich cultures of sulfolobus solfataricus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3958906/
https://www.ncbi.nlm.nih.gov/pubmed/24566144
http://dx.doi.org/10.3390/ijms15023204
work_keys_str_mv AT gogliettinomarta anewpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT riccioalessia anewpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT coccaennio anewpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT rossimose anewpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT palmierigianna anewpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT balestrierimarco anewpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT gogliettinomarta newpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT riccioalessia newpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT coccaennio newpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT rossimose newpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT palmierigianna newpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus
AT balestrierimarco newpepstatininsensitivethermopsinlikeproteaseoverproducedinpeptiderichculturesofsulfolobussolfataricus