Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus
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Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus (307 views)

Ruggiero I, Cantiello P, Lamberti A, Sorrentino A, Martucci NM, Ruggiero A, Arcone R, Vitagliano L, Arcari P, Masullo M

Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2009 Jul; 91(7): 835-842.

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Paper type: Journal Article,

Impact factor: 3.897, 5-year impact factor: 3.489

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-67349168130&partnerID=40&md5=f9dc6b28b4a765f3dd5f1da85c1a6132

Keywords: Elongation Factor 1α, Heat Stability, Mutagenic Analysis, Nucleotide Binding Site, Sulfolobus Solfataricus, Alanine, Amino Acid, Aspartic Acid, Carboxyl Group, Edetic Acid, Elongation Factor 1alpha, Guanosine Diphosphate, Guanosine Triphosphatase, Magnesium Ion, Mutant Protein, Nucleotide Derivative, Sodium Chloride, Amino Acid Analysis, Amino Acid Substitution, Archaebacterium, Bacterial Genetics, Binding Affinity, Catalysis, Controlled Study, Enzyme Activity, Genetic Conservation, Heterologous Expression, In Vitro Study, Nonhuman, Protein Folding, Protein Protein Interaction, Protein Synthesis, Thermostability, Wild Type, Genetic Vectors, Mutation, Peptide Elongation Factor 1, Protein Denaturation,

Affiliations:
*** IBB - CNR ***

Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II, Via S. Pansini 5, I-80131 Napoli, Italy
Dipartimento di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Complesso Ninì Barbieri, I-88021 Roccelletta di Borgia, CZ, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy


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Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus

The D60A mutant of the elongation factor (EF) 1α from Sulfolobus solfataricus (Ss), was obtained as heterologous expressed protein and characterised. This substitution was carried out in order to analyse the involvement of this evolutionally conserved amino acid position in the interaction between the elongation factor and guanosine nucleotides and in the coordination of magnesium ions. The expression system used produced a folded protein able to catalyse, although to a slightly lower extent with respect to the wild-type enzyme, protein synthesis in vitro and NaCl-dependent intrinsic GTPase activity. The affinity for guanosine nucleotides was almost identical to that exhibited by wild-type SsEF-1α; vice versa, the GDP exchange rate was one order of magnitude faster on the mutated elongation factor, a property partially restored when the exchange reaction was analysed in the presence of the magnesium ions chelating agent EDTA. Finally, the D60A substitution only a little affected the high thermal stability of the elongation factor. From a structural point of view, the analysis of the data reported confirmed that this conserved carboxyl group belongs to a protein region differentiating the GDP binding mode among elongation factors from different organisms. © 2009 Elsevier Masson SAS. All rights reserved.
Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus

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Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus

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Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
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Masullo M, Cantiello P, Paola B, Fiengo A, Vitagliano L, Zagari A, Arcari P
* Valine114 Replacements In The Archaeal Elongation Factor 1a Enhanced Its Ability To Interact With Aminoacyl-Trna And Kirromycin (352 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2002; 41(49): 14482-14488.
Impact Factor: 4.064
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Vitagliano L, Masullo M, Sica F, Zagari A, Bocchini V
* The crystal structure of Sulfolobus solfataricus elongation factor 1α in complex with GDP reveals novel features in nucleotide binding and exchange (452 views)
Embo J (ISSN: 0261-4189, 0261-4189linking), 2001 Oct 1; 20(19): 5305-5311.
Impact Factor: 12.459
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 Esposito L, Sica F, Sorrentino G, Berisio R, Carotenuto L, Giordano A, Raia C, Rossi M, Lamzin VS, Willson KS, Zagari A
Protein Crystal Growth In The Advance Protein Crystallisation Facility On The Lms Mission: A Comparison Of Sulfolobus Solfataricus Alchool Dehydrogenase Crystals Grown On The Ground And In Microgravity (253 views)
Acta Crystallogr D Biol Crystallogr, 1998; 54: 386-390.
Impact Factor: 0
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Esposito L, Sica F, Sorrentino G, Berisio R, Carotenuto L, Giordano A, Raia CA, Rossi M, Lamzin VS, Wilson KS, Zagari A
Protein crystal growth in the advanced protein crystallization facility on the LMS mission: A comparison of Sulfolobus solfataricus alcohol dehydrogenase crystals grown on the ground and in microgravity (433 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 1998; 54(3): 386-390.
Impact Factor: 2.244
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PEARL L, DEMASI D, HEMMINGS A, SICA F, MAZZARELLA L, RAIA C, DAURIA S, ROSSI M
CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF AN NAD+-DEPENDENT ALCOHOL-DEHYDROGENASE FROM THE EXTREME THERMOPHILIC ARCHAEBACTERIUM SULFOLOBUS-SOLFATARICUS (444 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1993 Feb 5; 229(3): 782-784.
Impact Factor: 5.673
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37 Records (37 excluding Abstracts).
Total impact factor: 127.814 (127.814 excluding Abstracts).
Total 5 year impact factor: 125.035 (125.035 excluding Abstracts).

Last modified by Marco Comerci on Sunday 12 July 2020, 13:15:01
307 views. Last view on Sunday 29 January 2023, 1:35:59