Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125

Extremophiles

Volumn 11, Issue 5, 2007, Pages 699-709

  Ruggiero, Immacolata ^a   Raimo, Gennaro ^a,b   Palma, Margherita ^a   Arcari, Paolo ^a   Masullo, Mariorosario ^a,c  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b UNIVERSITY OF MOLISE   (Italy)

^c UNIVERSITY MAGNA GRAECIA OF CATANZARO   (Italy)

Author keywords

Elongation factor G; GTPase; Heat stability; Pseudoalteromonas haloplanktis; Psychrophilic

Indexed keywords

ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; ELONGATION FACTOR G; FUSIDIC ACID; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PROTEIN SYNTHESIS INHIBITOR; RECOMBINANT PROTEIN;

ANTARCTICA; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; ENZYME STABILITY; ENZYMOLOGY; GENETICS; GROWTH, DEVELOPMENT AND AGING; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN SYNTHESIS; PSEUDOALTEROMONAS; RIBOSOME; TEMPERATURE;

ANTARCTIC REGIONS; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; CLONING, MOLECULAR; ENZYME STABILITY; FUSIDIC ACID; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MODELS, MOLECULAR; MOLECULAR WEIGHT; PEPTIDE ELONGATION FACTOR G; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN SYNTHESIS INHIBITORS; PSEUDOALTEROMONAS; RECOMBINANT PROTEINS; RIBOSOMES; TEMPERATURE;

ESCHERICHIA COLI; PSEUDOALTEROMONAS; PSEUDOALTEROMONAS HALOPLANKTIS; PSEUDOALTEROMONAS HALOPLANKTIS TAC125;

EID: 34548304992     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-007-0088-8     Document Type: Article

References (55)

1. Al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A (1996) The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure 15:555-565
2. Arai N, Arai K, Kaziro Y (1977) Further studies on the interaction of the polypeptide chain elongation factor G with guanine nucleotides. J Biochem (Tokyo) 82:687-694
3. Arai K, Arai N, Nakamura S, Oshima T, Kaziro Y (1978) Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. Eur J Biochem 92:521-531
4. Arcari P, Masullo M, Arcucci A, Ianniciello G, de Paola B, Bocchini V (1999) A chimeric elongation factor containing the putative guanine nucleotide binding domain of archaeal EF-1 alpha and the M and C domains of eubacterial EF-Tu. Biochemistry 38:12288-12295
5. Baca OG, Rohrbach MS, Bodley JW (1976) Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome. Biochemistry 15:4570-4574
6. Barrick D, Villanueba K, Childs J, Kalil R, Schneider TD, Lawrence CE, Gold L, Stormo GD (1994) Quantitative analysis of ribosome binding sites in E. coli. Nucleic Acids Res 22:1287-1295
7. Bhargava K, Templeton P, Spremulli LL (2004) Expression and characterization of isoform 1 of human mitochondrial elongation factor G. Protein Expr Purif 37:368-376
8. Birolo L, Tutino ML, Fontanella B, Gerday C, Mainolfi K, Pascarella S, Sannia G, Vinci F, Marino G (2000) Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties and molecular modelling. Eur J Biochem 267:2790-2802
9. Bocchetta M, Gribaldo S, Sanangelantoni A, Cammarano P (2000) Phylogenetic depth of the bacterial genera Aquifex and Thermotoga inferred from analysis of ribosomal protein, elongation factor, and RNA polymerase subunit sequences. J Mol Evol 50:366-380
10. Bodley JW, Zieve FJ, Lin L, Zieve ST (1969) Formation of the ribosome-G factor-GDP complex in the presence of fusidic acid. Biochem Biophys Res Commun 37:437-443
11. Bodley JW, Zieve FJ, Lin L, Zieve ST (1970) Studies on translocation. 3. Conditions necessary for the formation and detection of a stable ribosome-G factor-guanosine diphosphate complex in the presence of fusidic acid. J Biol Chem 245:5656-5661
12. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
13. Creti R, Ceccarelli E, Bocchetta M, Sanangelantoni AM, Tiboni O, Palm P, Cammarano P (1994) Evolution of translational elongation factor (EF) sequences: reliability of global phylogenies inferred from EF-1 alpha(Tu) and EF-2(G) proteins. Proc Natl Acad Sci USA 91:3255-3259
14. D'Amico S, Collins T, Marx JC, Feller G, Gerday C (2006) Psychrophilic microorganisms: challenges for life. EMBO Rep 7:385-389
15. De Vendittis E, Masullo M, Bocchini V (1986) The elongation factor G carries a catalytic site for GTP hydrolysis, which is revealed by using 2-propanol in the absence of ribosomes. J Biol Chem 261:4445-4450
16. De Vendittis E, Adinolfi BS, Amatruda MR, Raimo G, Masullo M, Bocchini V (1999) The A26G replacement in the consensus sequence A-X-X-X-X-G-K-[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus. Eur J Biochem 262:600-605
17. De Vendittis E, de Paola B, Gogliettino MA, Adinolfi BS, Fiengo A, Duvold T, Bocchini V (2002) Fusidic and helvolic acid inhibition of elongation factor 2 from the archaeon Sulfolobus solfataricus. Biochemistry 41:14879-14884
18. Dever TE, Glynias MJ, Merrick WC (1987) GTP-binding domain: three consensus sequence elements with distinct spacing. Proc Natl Acad Sci USA 84:1814-1818
19. Feller G, Gerday C (1997) Psychrophilic enzymes: molecular basis of cold adaptation. Cell Mol Life Sci 53:830-841
20. Feller G, Narinx E, Arpigny JL, Aittaleb M, Baise E, Gerday C (1996) Enzymes from psychrophilic organisms. FEMS Microbiol Rev 18:189-202
21. Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
22. Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT (2005) Structural insights into fusidic acid resistance and sensitivity in EF-G. J Mol Biol 348:939-949
23. Herbert RA, Sharp RS (1992) Molecular biology and biotechnology of extremophiles. Blakie Press, New York, USA
24. Hoyoux A, Blaise V, Collins T, D'Amico S, Gratia E, Huston AL, Marx JC, Sonan G, Zeng Y, Feller G, Gerday C (2004) Extreme catalysts from low-temperature environments. J Biosci Bioeng 98:317-330
25. Jaenicke R, Zavodszky P (1990) Proteins under extreme physical conditions. FEBS Lett 268:344-349
26. Johanson U, Hughes D (1994) Fusidic acid-resistant mutants define three regions in elongation factor G of Salmonella typhimurium. Gene 143:55-59
27. Johanson U, Aevarsson A, Liljas A, Hughes D (1996) The dynamic structure of EF-G studied by fusidic acid resistance and internal revertants. J Mol Biol 258:420-432
28. Kaziro Y (1978) The role of guanosine 5′-triphosphate in polypeptide chain elongation. Biochim Biophys Acta 505:95-127
29. Klink F (1985) Elongation factors. In: Woese CR, Wolfe R (eds) The bacteria, vol 8. Academic, London, pp 379-410
30. Lucas-Lenard J (1971) Protein biosynthesis. Annu Rev Biochem 40:409-448
31. Martemyanov KA, Liljas A, Yarunin AS, Gudkov AT (2001) Mutations in the G-domain of elongation factor G from Thermus themophilus affect both its interaction with GTP and fusidic acid. J Biol Chem 276:28774-28778
32. Masullo M, Parlato G, De Vendittis E, Bocchini V (1989) Effect of propan-2-ol on enzymic and structural properties of elongation factor G. Biochem J 261:725-731
33. Masullo M, De Vendittis E, Bocchini V (1994) Archaebacterial elongation factor 1 alpha carries the catalytic site for GTP hydrolysis. J Biol Chem 269:20376-20379
34. Masullo M, Arcari P, de Paola B, Parmeggiani A, Bocchini V (2000) Psychrophilic elongation factor Tu from the Antarctic Pseudoalteromonas haloplanktis sp. TAC II 25. Biochemical characterization and cloning of the encoding gene. Biochemistry 39:15531-15539
35. Medigue C, Krin E, Pascal G, Barbe V, Bernsel A, Bertin PN, Cheung F, Cruveiller S, D'Amico S, Duilio A, Fang G, Feller G, Ho C, Mangenot S, Marino G, Nilsson J, Parrilli E, Rocha EP, Rouy Z, Sekowska A, Tutino ML, Vallenet D, von Heijne G, Danchin A (2005) Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125. Genome Res 15:1325-1335
36. Miller DL, Weissbach H (1977) In: Weissbach H, Pestka S (eds) Molecular mechanisms of protein biosynthesis. Academic, New York, pp 323-373
37. Nagaev I, Bjorkman J, Andersson DI, Hughes D (2001) Biological cost and compensatory evolution in fusidic acid-resistant Staphylococcus aureus. Mol Microbiol 40:433-439
38. Parmeggiani A, Sander G (1981) Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2. Mol Cell Biochem 35:129-158
39. Peitsch MC (1996) ProMod and Swiss-Model: internet-based tools for automated comparative protein modeling. Biochem Soc Trans 24:274-279
40. Peske F, Savelsbergh A, Katunin VI, Rodnina MV, Wintermeyer W (2004) Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation. J Mol Biol 343:1183-1194
41. Post LE, Nomura N (1980) DNA sequences from the str operon of Escherichia coli. J Biol Chem 255:4660-4666
42. Pribnow D (1975) Bacteriophage T7 early promoters: nucleotide sequences of two RNA polymerase binding sites. J Mol Biol 99:419-433
43. Raimo G, Masullo M, Parente A, Dello Russo A, Bocchini V (1992) Molecular, functional and structural properties of an archaebacterial elongation factor 2. Biochim Biophys Acta 1132:127-132
44. Raimo G, Masullo M, Bocchini V (1995) Studies on the polypeptide elongation factor 2 from Sulfolobus solfataricus. Interaction with guanosine nucleotides and GTPase activity stimulated by ribosomes. J Biol Chem 270:21082-21085
45. Raimo G, Masullo M, Scarano G, Bocchini V (1996) The site for GTP hydrolysis on the archaeal elongation factor 2 is unmasked by aliphatic alcohols. Biochimie 78:832-837
46. Raimo G, Lombardo B, Masullo M, Lamberti A, Longo O, Arcari P (2005) Elongation factor Ts from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC125: biochemical characterization and cloning of the encoding gene. Biochemistry 43:14759-14766
47. Sander G, Marsh RC, Voigt J, Parmeggiani A (1975) A comparative study of the 50S ribosomal subunit and several 50S subparticles in EF-T-and EF-G-dependent activities. Biochemistry 14:1805-1814
48. Shine J, Dalgarno L (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci USA 71:1342-1346
49. Siddiqui KS, Cavicchioli R (2006) Cold-adapted enzymes. Annu Rev Biochem 26:403-433
50. Stark H, Rodnina MV, Wieden HJ, van Heel M, Wintermeyer W (2000) Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell 100:301-309
51. Tanford C (1962) Contribution of hydrophobic interactions to the stability of the globular conformation of proteins. J Am Chem Soc 84:4240-4247
52. Thomas T, Cavicchioli R (2000) Effect of temperature on stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens. J Bacteriol 182:1328-1332
53. Tosco A, Birolo L, Madonna S, Lolli G, Sannia G, Marino G (2003) GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: molecular characterization and gene cloning. Extremophiles 7:17-28
54. Willie GR, Richman N, Godtfredsen WO, Bodley JW (1975) Some characteristics of and structural requirements for the interaction of 24,25-dihydrofusidic acid with ribosome-elongation factor G complexes. Biochemistry 14:1713-1718
55. Zuber H (1988) Temperature and adaptation of lactate dehydrogenase. Structural, functional and genetic aspects. Biophys Chem 29:171-179