Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene
The elongation factor Ts was isolated from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 strain (PhEF-Ts), and its functional properties were studied. At 0 °C PhEF-Ts enhanced the [3H]GDP/GDP exchange rate on the preformed PhEF-Tuâ[3H]GDP complex by 2 orders of magn...
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ftunivmoliseiris:oai:iris.unimol.it:11695/8168 2024-04-14T08:01:47+00:00 Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene RAIMO, Gennaro LOMBARDO B. MASULLO M. LAMBERTI A. LONGO O. AND ARCARI P. Raimo, Gennaro Lombardo, B. Masullo, M. Lamberti, A. Longo, O. AND ARCARI, P. 2004 http://hdl.handle.net/11695/8168 eng eng info:eu-repo/semantics/altIdentifier/wos/000225172800026 volume:43 firstpage:14759 lastpage:14766 numberofpages:8 journal:BIOCHEMISTRY http://hdl.handle.net/11695/8168 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-8744268550 elongation factor T Pseudoalteromonas haloplankti enzyme cold adaptation info:eu-repo/semantics/article 2004 ftunivmoliseiris 2024-03-21T18:04:21Z The elongation factor Ts was isolated from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 strain (PhEF-Ts), and its functional properties were studied. At 0 °C PhEF-Ts enhanced the [3H]GDP/GDP exchange rate on the preformed PhEF-Tuâ[3H]GDP complex by 2 orders of magnitude even at very low Tu:Ts ratio, by lowering the energy of activation of the exchange reaction. PhEF-Ts is a monomeric protein, and in solution it forms a stable dimeric complex with PhEFTu. The PhEF-Ts encoding gene was cloned and sequenced. Its structural organization was similar to that of Escherichia coli because it showed at its 5¢ end the gene encoding the ribosomal protein S2. The translated amino acid sequence had a calculated molecular weight of 30762, and showed a high sequence identity with E. coli (68%) and Thermus thermophilus (44%) EF-Ts. The PhEF-Ts primary structure contains well-preserved almost all the amino acid residues interacting at the interfaces of the E. coli EF-TsâEF-Tu complex. Finally, the high concentration of PhEF-Ts in this psychrophilic eubacterium might represent an adaptive tool to ensure an efficient nucleotide exchange even at low temperature. 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 |
institution |
Open Polar |
collection |
Università degli Studi del Molise: IRIS |
op_collection_id |
ftunivmoliseiris |
language |
English |
topic |
elongation factor T Pseudoalteromonas haloplankti enzyme cold adaptation |
spellingShingle |
elongation factor T Pseudoalteromonas haloplankti enzyme cold adaptation RAIMO, Gennaro LOMBARDO B. MASULLO M. LAMBERTI A. LONGO O. AND ARCARI P. Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene |
topic_facet |
elongation factor T Pseudoalteromonas haloplankti enzyme cold adaptation |
description |
The elongation factor Ts was isolated from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 strain (PhEF-Ts), and its functional properties were studied. At 0 °C PhEF-Ts enhanced the [3H]GDP/GDP exchange rate on the preformed PhEF-Tuâ[3H]GDP complex by 2 orders of magnitude even at very low Tu:Ts ratio, by lowering the energy of activation of the exchange reaction. PhEF-Ts is a monomeric protein, and in solution it forms a stable dimeric complex with PhEFTu. The PhEF-Ts encoding gene was cloned and sequenced. Its structural organization was similar to that of Escherichia coli because it showed at its 5¢ end the gene encoding the ribosomal protein S2. The translated amino acid sequence had a calculated molecular weight of 30762, and showed a high sequence identity with E. coli (68%) and Thermus thermophilus (44%) EF-Ts. The PhEF-Ts primary structure contains well-preserved almost all the amino acid residues interacting at the interfaces of the E. coli EF-TsâEF-Tu complex. Finally, the high concentration of PhEF-Ts in this psychrophilic eubacterium might represent an adaptive tool to ensure an efficient nucleotide exchange even at low temperature. |
author2 |
Raimo, Gennaro Lombardo, B. Masullo, M. Lamberti, A. Longo, O. AND ARCARI, P. |
format |
Article in Journal/Newspaper |
author |
RAIMO, Gennaro LOMBARDO B. MASULLO M. LAMBERTI A. LONGO O. AND ARCARI P. |
author_facet |
RAIMO, Gennaro LOMBARDO B. MASULLO M. LAMBERTI A. LONGO O. AND ARCARI P. |
author_sort |
RAIMO, Gennaro |
title |
Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene |
title_short |
Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene |
title_full |
Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene |
title_fullStr |
Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene |
title_full_unstemmed |
Elongation Factor Ts from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125: Biochemical Characterisation, and Cloning of the Encoding Gene |
title_sort |
elongation factor ts from the antarctic eubacterium pseudoalteromonas haloplanktis tac 125: biochemical characterisation, and cloning of the encoding gene |
publishDate |
2004 |
url |
http://hdl.handle.net/11695/8168 |
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/000225172800026 volume:43 firstpage:14759 lastpage:14766 numberofpages:8 journal:BIOCHEMISTRY http://hdl.handle.net/11695/8168 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-8744268550 |
_version_ |
1796310777116753920 |