Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125
The molecular and functional properties of the elongation factor (EF) G from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph) were studied. PhEF-G catalyzed protein synthesis in vitro that was inhibited by fusidic acid, an antibiotic specifically acting on EF-G. The EF int...
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ftunivmoliseiris:oai:iris.unimol.it:11695/3540 2024-04-14T08:04:19+00:00 Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 Ruggiero, I Palma, M Arcari, P Masullo, M. RAIMO, Gennaro Ruggiero, I Raimo, Gennaro Palma, M Arcari, P Masullo, M. 2007 http://hdl.handle.net/11695/3540 https://doi.org/10.1007/s00792-007-0088-8 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000249119300007 volume:5 firstpage:699 lastpage:709 numberofpages:11 journal:EXTREMOPHILES http://hdl.handle.net/11695/3540 doi:10.1007/s00792-007-0088-8 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34548304992 elongation factor G GTPase Heat stability Psychrophilic Pseudoalteromonas haloplanktis info:eu-repo/semantics/article 2007 ftunivmoliseiris https://doi.org/10.1007/s00792-007-0088-8 2024-03-21T18:07:17Z The molecular and functional properties of the elongation factor (EF) G from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph) were studied. PhEF-G catalyzed protein synthesis in vitro that was inhibited by fusidic acid, an antibiotic specifically acting on EF-G. The EF interacted with GDP only in the presence of P. haloplanktis ribosome and fusidic acid with an affinity similar to that displayed by Escherichia coli EFG. The psychrophilic translocase elicited a ribosomedependent GTPase that was competitively inhibited by GDP, the slowly hydrolyzable GTP analog GppNHp, and the protein synthesis inhibitor ppGDP. The temperature dependence of the activity of PhEF-G reached its maximum at least 26C beyond the growth temperature of P. haloplanktis (4–20C). The heat inactivation profile of the ribosome-dependent GTPase of PhEF-G gave a temperature for half inactivation (46C), significantly lower than that for half denaturation measured by either UV- (57C) or fluorescence-melting (62C). This finding was attributed to a different effect of the temperature on the catalytic domain with respect to that elicited on the other domains constituting the EF, thus confirming the differential molecular flexibility present in psychrophilic enzymes. A molecular model, based on the 3D coordinates of a thermophilic Article in Journal/Newspaper Antarc* Antarctic Università degli Studi del Molise: IRIS Antarctic Tac ENVELOPE(-59.517,-59.517,-62.500,-62.500) The Antarctic Extremophiles 11 5 699 709 |
institution |
Open Polar |
collection |
Università degli Studi del Molise: IRIS |
op_collection_id |
ftunivmoliseiris |
language |
English |
topic |
elongation factor G GTPase Heat stability Psychrophilic Pseudoalteromonas haloplanktis |
spellingShingle |
elongation factor G GTPase Heat stability Psychrophilic Pseudoalteromonas haloplanktis Ruggiero, I Palma, M Arcari, P Masullo, M. RAIMO, Gennaro Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
topic_facet |
elongation factor G GTPase Heat stability Psychrophilic Pseudoalteromonas haloplanktis |
description |
The molecular and functional properties of the elongation factor (EF) G from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph) were studied. PhEF-G catalyzed protein synthesis in vitro that was inhibited by fusidic acid, an antibiotic specifically acting on EF-G. The EF interacted with GDP only in the presence of P. haloplanktis ribosome and fusidic acid with an affinity similar to that displayed by Escherichia coli EFG. The psychrophilic translocase elicited a ribosomedependent GTPase that was competitively inhibited by GDP, the slowly hydrolyzable GTP analog GppNHp, and the protein synthesis inhibitor ppGDP. The temperature dependence of the activity of PhEF-G reached its maximum at least 26C beyond the growth temperature of P. haloplanktis (4–20C). The heat inactivation profile of the ribosome-dependent GTPase of PhEF-G gave a temperature for half inactivation (46C), significantly lower than that for half denaturation measured by either UV- (57C) or fluorescence-melting (62C). This finding was attributed to a different effect of the temperature on the catalytic domain with respect to that elicited on the other domains constituting the EF, thus confirming the differential molecular flexibility present in psychrophilic enzymes. A molecular model, based on the 3D coordinates of a thermophilic |
author2 |
Ruggiero, I Raimo, Gennaro Palma, M Arcari, P Masullo, M. |
format |
Article in Journal/Newspaper |
author |
Ruggiero, I Palma, M Arcari, P Masullo, M. RAIMO, Gennaro |
author_facet |
Ruggiero, I Palma, M Arcari, P Masullo, M. RAIMO, Gennaro |
author_sort |
Ruggiero, I |
title |
Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_short |
Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_full |
Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_fullStr |
Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_full_unstemmed |
Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 |
title_sort |
molecular and functional properties of the psychrophilic elongation factor g from the antarctic eubacterium pseudoalteromonas haloplanktis tac 125 |
publishDate |
2007 |
url |
http://hdl.handle.net/11695/3540 https://doi.org/10.1007/s00792-007-0088-8 |
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/wos/WOS:000249119300007 volume:5 firstpage:699 lastpage:709 numberofpages:11 journal:EXTREMOPHILES http://hdl.handle.net/11695/3540 doi:10.1007/s00792-007-0088-8 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34548304992 |
op_doi |
https://doi.org/10.1007/s00792-007-0088-8 |
container_title |
Extremophiles |
container_volume |
11 |
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5 |
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709 |
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