Two homologous EF-G proteins from Pseudomonas aeruginosa exhibit distinct functions

PLoS ONE

Volumn 8, Issue 11, 2013, Pages

  Palmer, Stephanie O ^a   Rangel, Edna Y ^a   Hu, Yanmei ^a   Tran, Alexis T ^a   Bullard, James M ^a  

^a UNIVERSITY OF TEXAS PAN AMERICAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; ELONGATION FACTOR G1A; ELONGATION FACTOR G1B; FUSIDIC ACID; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; PHENYLALANINE; POLYURIDYLIC ACID; RIBOSOME RECYCLING FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GENOME; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; GENE LOCATION; HYDROLYSIS; KINETICS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; POLYMERIZATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; PSEUDOMONAS AERUGINOSA; RIBOSOME; RNA TRANSLATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

BACTERIAL PROTEINS; FUSIDIC ACID; GTP PHOSPHOHYDROLASES; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; KINETICS; PEPTIDE ELONGATION FACTOR G; POLY U; PSEUDOMONAS AERUGINOSA; RIBOSOMES; SEQUENCE ANALYSIS;

EID: 84892582098     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080252     Document Type: Article

References (41)

1. Conway TW, Lipmann F (1964) Characterization of a ribosome-linked guanosine triphosphatase in Escherichia coli extracts. Proc Natl Acad Sci U-S-A 52: 1462-1469. doi:10.1073/pnas.52.6.1462. PubMed: 14243519.
2. Bourne HR, Sanders DA, McCormick F (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117-127. doi:10.1038/349117a0. PubMed: 1898771.
3. Nishizuka Y, Lipmann F (1966) Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system. Proc Natl Acad Sci U-S-A 55: 212-219. doi:10.1073/pnas.55.1.212. PubMed: 4287350.
4. Alakhov YB, Dovgas NV, Motuz LP, Vinokurov LM, Ovchinnikov YA (1981) The primary structure of the elongation factor G from Escherichia coli: amino acid sequence of the C-terminal domain. FEBS Lett 126: 183-186. doi:10.1016/0014- 5793(81)80237-2. PubMed: 7016587.
5. De VE, 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. PubMed: 3007457.
6. Czworkowski J, Wang J, Steitz TA, Moore PB (1994) The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J 13: 3661-3668. PubMed: 8070396.
7. AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y et al. (1994) Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J 13: 3669-3677. PubMed: 8070397.
8. Rodnina MV, Savelsbergh A, Katunin VI, Wintermeyer W (1997) Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385: 37-41. doi:10.1038/385037a0. PubMed: 8985244.
9. Rodnina MV, Wintermeyer W (2011) The ribosome as a molecular machine: the mechanism of tRNA-mRNA movement in translocation. Biochem Soc Trans 39: 658-662. doi:10.1042/BST0390658. PubMed: 21428957.
10. Frank J, Gao H, Sengupta J, Gao N, Taylor DJ (2007) The process of mRNA-tRNA translocation. Proc Natl Acad Sci U-S-A 104: 19671-19678. doi:10.1073/pnas.0708517104. PubMed: 18003906.
11. Hirashima A, Kaji A (1973) Role of elongation factor G and a protein factor on the release of ribosomes from messenger ribonucleic acid. J Biol Chem 248: 7580-7587. PubMed: 4583357.
12. Zavialov AV, Hauryliuk VV, Ehrenberg M (2005) Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G. Mol Cell 18: 675-686. doi:10.1016/j.molcel.2005.05.016. PubMed: 15949442.
13. Hammarsund M, Wilson W, Corcoran M, Merup M, Einhorn S et al. (2001) Identification and characterization of two novel human mitochondrial elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved through evolution. Hum Genet 109: 542-550. doi:10.1007/s00439-001-0610-5. PubMed: 11735030.
14. 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. doi:10.1016/j.pep.2004.06.030. PubMed: 15358359.
15. mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol Cell 35: 502-510. doi:10.1016/j.molcel.2009.06.028. PubMed: 19716793.
16. Margus T, Remm M, Tenson T (2007) Phylogenetic distribution of translational GTPases in bacteria. BMC Genomics 8: 15-33. doi: 10.1186/1471-2164-8-15. PubMed: 17214893.
17. Connell SR, Takemoto C, Wilson DN, Wang H, Murayama K et al. (2007) Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors. Mol Cell 25: 751-764. doi: 10.1016/j.molcel.2007. 01.027. PubMed: 17349960.
18. Seshadri A, Samhita L, Gaur R, Malshetty V, Varshney U (2009) Analysis of the fusA2 locus encoding EFG2 in Mycobacterium smegmatis. Tuberculosis (Edinb.) 89: 453-464.
19. Suematsu T, Yokobori SI, Morita H, Yoshinari S, Ueda T et al. (2010) A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi. Mol Microbiol 75: 1445-1454. doi:10.1111/j.1365-2958.2010.07067.x. PubMed: 20132446.
20. Roussel P, Lamblin G (2003) The glycosylation of airway mucins in cystic fibrosis and its relationship with lung infection by Pseudomonas aeruginosa. Adv Exp Med Biol 535: 17-32. doi: 10.1007/978-1-4615-0065-0-2. PubMed: 14714886.
21. Atkinson GC, Baldauf SL (2011) Evolution of elongation factor G and the origins of mitochondrial and chloroplast forms. Mol Biol Evol 28: 1281-1292. doi:10.1093/molbev/msq316. PubMed: 21097998.
22. Tam MF, Dodd JA, Hill WE (1981) Physical characteristics of 16 S rRNA under reconstitution conditions. J Biol Chem 256: 6430-6434. PubMed: 6165717.
23. 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. doi: 10.1016/0003-2697(76)90527-3. PubMed: 942051.
24. Cull MG, McHenry CS (1995) Purification of Escherichia coli DNA polymerase III holoenzyme. Methods Enzymol 262: 22-35. doi: 10.1016/0076- 6879(95)62005-2. PubMed: 8594350.
25. Bullard JM, Williams JC, Acker WK, Jacobi C, Janjic N et al. (2002) DNA polymerase III holoenzyme from Thermus thermophilus identification, expression, purification of components, and use to reconstitute a processive replicase. J Biol Chem 277: 13401-13408. doi:10.1074/jbc.M110833200. PubMed: 11823461.
26. Nyfeler B, Hoepfner D, Palestrant D, Kirby CA, Whitehead L et al. (2012) Identification of elongation factor G as the conserved cellular target of argyrin B. PLOS ONE. 7: e42657. doi:10.1371/journal.pone. 0042657. PubMed: 22970117.
27. Jurnak F (1994) The ABC of EF-G. Structure. 2: 785-788. doi:10.1016/S0969-2126(94)00078-6. PubMed: 7812711.
28. Nechifor R, Murataliev M, Wilson KS (2007) Functional interactions between the G' subdomain of bacterial translation factor EF-G and ribosomal protein L7/L12. J Biol Chem 282: 36998-37005. doi:10.1074/jbc.M707179200. PubMed: 17932030.
29. 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. doi: 10.1016/0006-291X(69)90934-6. PubMed: 4900137.
30. Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC et al. (2009) The structure of the ribosome with elongation factor G trapped in the post-translocational state. Science 326: 694-699. doi:10.1126/science.1179709. PubMed: 19833919.
31. Martemyanov KA, Liljas A, Yarunin AS, Gudkov AT (2001) Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid. J Biol Chem 276: 28774-28778. doi:10.1074/jbc.M102023200. PubMed: 11371559.
32. 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. doi:10.1016/j.jmb.2005.02.066. PubMed: 15843024.
33. Johanson U, Hughes D (1994) Fusidic acid-resistant mutants define three regions in elongation factor G of Salmonella typhimurium. Gene 143: 55-59. doi:10.1016/0378-1119(94)90604-1. PubMed: 7515367.
34. Chen Y, Koripella RK, Sanyal S, Selmer M (2010) Staphylococcus aureus elongation factor G - structure and analysis of a target for fusidic acid. FEBS J 277: 3789-3803. doi:10.1111/j.1742-4658.2010.07780.x. PubMed: 20718859.
35. Palmer SO, Rangel EY, Montalvo AE, Tran AT, Ferguson KC et al. (2013) Cloning and characterization of EF-Tu and EF-Ts from Pseudomonas aeruginosa. Biomed Res International 2013: Article ID 585748 doi:10.1155/2013/585748. PubMed: 23984384.
36. Mosteller RC, Culp WJ, Hardesty B (1968) The requirement for tRNA for the shift in the optimum Mg ++ concentration during the synthesis of polyphenylalanine. Biochem Biophys Res Commun 30: 631-636. doi: 10.1016/0006-291X(68)90559-7. PubMed: 5642381.
37. Ribble W, Hill WE, Ochsner UA, Jarvis TC, Guiles JW et al. (2010) Discovery and analysis of 4H-pyridopyrimidines, a class of selective bacterial protein synthesis inhibitors. Antimicrob Agents Chemother 54: 4648-4657. doi:10.1128/AAC.00638-10. PubMed: 20696870.
38. Margus T, Remm M, Tenson T (2011) A computational study of elongation factor G (EFG) duplicated genes: diverged nature underlying the innovation on the same structural template. PLOS ONE 6: e22789. doi:10.1371/journal.pone. 0022789. PubMed: 21829651.
39. Bielecki P, Lukat P, Hüsecken K, Dötsch A, Steinmetz H et al. (2012) Mutation in elongation factor G confers resistance to the antibiotic argyrin in the opportunistic pathogen Pseudomonas aeruginosa. Chembiochem 13: 2339-2345. doi:10.1002/cbic.201200479. PubMed: 23011873.
40. An D, Parsek MR (2007) The promise and peril of transcriptional profiling in biofilm communities. Curr Opin Microbiol 10: 292-296. doi: 10.1016/j.mib.2007.05.011. PubMed: 17573234.
41. Moreau-Marquis S, Stanton BA, O'Toole GA (2008) Pseudomonas aeruginosa biofilm formation in the cystic fibrosis airway. Pulm Pharmacol Ther 21: 595-599. doi:10.1016/j.pupt.2007.12.001. PubMed: 18234534.