博碩士論文 105821602 詳細資訊




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姓名 阮越康(Nguyen Viet Khang)  查詢紙本館藏   畢業系所 生命科學系
論文名稱 蘇雲金芽孢桿菌含有兩種Prolyl-tRNA synthetase基因
(Bacillus thuringiensis possesses two prolyl-tRNA synthetase genes of distinct origins)
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摘要(中) Prolyl-tRNA synthetase (ProRS)是一種第二類型tRNA合成酶,按照序列分析兩種不同構造的ProRS存在於不同物種中:原核型與真核型。多數細菌只含有一種原核型ProRS基因,但蘇雲金芽孢桿菌含有兩種ProRS基因:proS1與proS2。令人驚奇的是,這兩種基因擁有不同的來源,且proS1的表現量遠大於proS2。根據同源tRNAPro的辨識部位,proS1應該是構造性基因,但proS2的功能則未知。這個多出來的proS2基因猜測是來自於基因水平轉移 (HGT),其所解碼的蛋白質可能在逆境中拯救proS1功能或參與含proline抗生素的合成。至於蘇雲金芽孢桿菌是如何將proline接到其對應tRNA上的機制,我們尚未能做完整解釋。ProRS的親源演化分析告訴我們,蘇雲金芽孢桿菌ProRS2和植物ProRS2有很高的序列同源性。另外,這細菌被發現和橄欖樹 (Olea europaea)有共生關係,這個發現暗示proS2基因可能是為了生存必須而從橄欖樹水平轉移過來的可能性。探討兩物種之間的生物相剋相生關係可以讓我們更加了解生物水平轉移的機制,也能對於ProRS的抑制機制獲得進一步的解釋。
摘要(英) Prolyl-tRNA synthetase (ProRS) is a class II synthetase which, according to sequence analysis, occurs in various organisms with one of two distinct structural architectures: prokaryotic-like and eukaryotic-like. While most of bacteria contain only one prokaryotic-like ProRS gene, Bacillus thuringiensis possesses two ProRS genes: proS1 and proS2. Intriguingly, both genes have different origins in which the expression of proS1 is much higher than that of proS2. Based on cognate tRNAPro identity elements, proS1 is supposed to be constitutive, whereas the function of proS2 remains unclear. The additional proS2 gene is hypothesized to be acquired by horizontal gene transfer (HGT) whose encoded protein (ProRS2) probably plays essential roles in rescuing the function of proS1 during stress conditions, participating in the biosynthetic pathways of antibiotics containing proline moiety, maintaining faithful translation. The question of how B. thuringiensis ProRS2 charges proline to its cognate tRNA remains to be characterized. The phylogenetic analysis of ProRS sequences showed that B. thuringiensis ProRS2 is well-aligned with plant ProRSs. The bacterium, additionally, can live symbiotically with olive tree (Olea europaea), raising a possibility that proS2 was transferred horizontally from the host tree during evolution course due to the necessity for survival. Understanding the allelopathic relationship between the two species could gain insight not only into the mechanism of HGT, but also into the inhibition of ProRSs.
關鍵字(中) ★ 蘇雲金芽孢桿菌
★ 基因水平轉移
★ 欖樹
關鍵字(英) ★ Prolyl-tRNA synthetase
★ Horizontal gene transfer
★ Olive
論文目次 中文摘要 i
Abstract ii
Acknowledgement iii
Table of Contents iv
List of Figures and Tables v
Abbreviations vi
1. Introduction 1
1.1 ProRS family is divided into two evolutionarily distinct groups 1
1.2 Different ProRS types recognize different tRNAsPro 1
1.3 Bacillus thuringiensis possesses two paralogous ProRSs 2
2. Materials and methods 4
2.1 Strains and culture medium 4
2.2 Preparation and transformation of E. coli competent cells 5
2.3 Preparation and transformation of yeast competent cells 7
2.4 Construction of BtProRSs 8
2.5 Protein preparation 8
2.6 SDS-PAGE 9
2.7 Western blot 10
2.8 Purification of His6-tagged proteins 12
2.9 Reverse-transcription (RT)-PCR 14
3. Results 16
3.1 B. thuringiensis contains two paralogous ProRSs and one p-type tRNAPro 16
3.2 Expression levels of B. thuringiensis ProRS genes under stress conditions 17
3.3 A proposed evolutionary history of ProRS 18
3.4 Why does B. thuringiensis possess two ProRSs? 20
4. Discussion 22
5. Reference 25
Figures 29
Supplementary Table 41
參考文獻 1. Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H., Hartsch T. and Söll D. (2002) Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases. J. Biol. Chem. 277, 34743–34748.
2. An S. and Musier-Forsyth K. (2004) Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK protein. J. Biol. Chem. 279, 42359–42362.
3. Argôlo-Filho R. C. and Loguercio L. L. (2013) Bacillus thuringiensis is an environmental pathogen and host-specificity has developed as an adaptation to human-generated ecological niches. Insects. 1, 62-91.
4. Beuning P. J. and Musier-Forsyth K. (2000) Hydrolytic editing by a class II aminoacyl-tRNA synthetase. Proc. Natl. Acad. Sci. U.S.A. 97, 8916–8920
5. Bunjun S., Stathopoulos C., Graham D., Min B., Kitabatake M., Wang A. L., Wang C. C., Vivarès C. P., Weiss L. M., Söll D. (2000) A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lamblia. Proc Natl Acad Sci U S A. 24, 12997-13002.
6. Burbaum J. J., Schimmel P. (1991) Structural relationships and the classification of aminoacyl-tRNA synthetases. J. Biol. Chem. 266, 16965-16968.
7. Burke B., Lipman R.S., Shiba K., Musier-Forsyth K. and Hou Y. M. (2001) Divergent adaptation of tRNA recognition by Methanococcus jannaschii prolyl-tRNA synthetase. J Biol Chem. 23, 20286-20291.
8. Carter C. W. Jr. (1993) Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases. Annu. Rev. Biochem. 62, 715-748.
9. Chen S. J., Wu Y. H., Huang H. Y., Wang C. C. (2012) Saccharomyces cerevisiae possesses a stress-inducible glycyl-tRNA synthetase gene. PLoS One. 7, e33363.
10. Chien C. I., Chen Y. L., Chen S. J., Chou C. M., Chen C. Y. and Wang C. C. (2015) Vanderwaltozyma polyspora possesses two glycyl-tRNA synthetase genes: one constitutive and one inducible. Fungal Genet Biol. 76, 47-56.
11. Clark R. L. and Neidhardt F. C. (1990) Roles of two lysyl-tRNA synthetases of Escherichia coli: analysis of nucleotide sequences and mutant behavior. J. Bacteriol. 172, 3237-3243.
12. Cinar C., Apaydin O., Yenidunya A.F., Harsa S., Gunes H. (2008) Isolation and characterization of Bacillus thuringiensis strains from olive-related habitats in Turkey. J. Appl. Microbiol. 104, 515-525.
13. Cusack S, Hartlein M, Leberman R (1991) Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 19, 3489-3498.
14. Fan F., Vetting M. W., Frantom P. A. and Blanchard J. S. (2009) Structures and mechanisms of the mycothiol biosynthetic enzymes. Curr Opin Chem Biol. 4, 451-459.
15. Feng L., Stathopoulos C., Ahel I., Mitra A., Tumbula-Hansen D., Hartsch T., Söll D. (2002) Aminoacyl-tRNA formation in the extreme thermophile Thermus thermophilus. Extremophiles. 2, 167-174.
16. Ibba M., Francklyn C. and Cusack S. (2005) The aminoacyl-tRNAsynthetases. CRC Press, Georgetown, Tex., U.S.A.
17. Garg R. P. and Parry R. J. (2010) Regulation of valanimycin biosynthesis in Streptomyces viridifaciens: characterization of VlmI as a Streptomyces antibiotic regulatory protein (SARP). Microbiol. 156, 472-483.
18. Giegé R., Sissler M., Florentz C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res. 26, 5017-5035.
19. Guo M., Xiang X. L., Schimmel P. (2010) New functions of aminoacyl-tRNA synthetases beyond translation. Nat Rev Mol Cell Biol. 9, 668-674.
20. Kitabatake M., Ali K., Demain A., Sakamoto K., Yokoyama S., Söll D. (2002) Indolmycin resistance of Streptomyces coelicolor A3(2) by induced expression of one of its two tryptophanyl-tRNA synthetases. J. Biol. Chem. 26, 23882-23887.

21. Lee J., Joshi N., Pasini R., Dobson R. C., Allison J. and Leustek T. (2016) Inhibition of Arabidopsis growth by the allelopathic compound azetidine-2-carboxylate is due to the low amino acid specificity of cytosolic prolyl-tRNA synthetase. Plant J. 88, 236-246
22. Liu H., Peterson R., Kessler J. et al. (1995) Molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase in vitro. Nucleic Acids Res. 23, 165-169.
23. Maria-Elena T., Wittung E. P. L., Alison D. H., Talal S. H. and Miller A. D. (1996) Characterisation of stress protein LysU. Enzymic synthesis of diadenosine 5’,5’’’-P1,P4-tetraphosphate (Ap4A) analogues by LysU. J. Chem. Soc. 0, 2009-2019.
24. McClain W. H., Schneider J, Gabriel K (1994) Distinctive acceptor-end structure and other determinants of Escherichia coli tRNAPro identity. Nucleic Acids Res. 22, 522-529.
25. O’Donoghue P. and Luthey-Schulten Z. (2003) On the evolution of structure in aminoacyl-tRNA synthetases. Microbiol Mol Biol Rev. 4, 550-573.
26. Oliynyk M., Samborskyy M., Lester J. B., Mironenko T., Scott N., Dickens S., Haydock S. F., and Leadlay P. F. (2007) Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL 23338. Nat. Biotechnol. 25, 447-453.
27. Ray P. S., Sullivan J. C., Jia J., Francis J., Finnerty J. R. and Fox P. L. (2011) Evolution of function of a fused metazoan tRNA synthetase. Mol Biol Evol. 1, 437-447
28. Ribas de Pouplana L. and Schimmel P. (2001) Aminoacyl-tRNA synthetases: potential markers of genetic code development. Trends Biochem Sci. 10, 591-596.
29. Shannon M. S., Huang J. L., Johann P. G. (2015) Horizontal gene transfer: building the web of life. Nat. 16, 472-482.
30. Splan K. E., Ignatov M. E. and Musier-Forsyth K. (2008) Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase. J. Biol. Chem. 283, 7128–7134
31. Stathopoulos C., Kim W., Li T., Anderson I., Deutsch B., Palioura S., Whitman W., Söll D. (2001) Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis. Proc Natl Acad Sci U S A. 25, 14292-14297.
32. Stehlin C, Bruke B, Yang F et al. (1998) Species-specific differences in the operational RNA code for aminoacylation of tRNAPro. Biochem. 37, 8605-8613.
33. SternJohn J., Hati S., Siliciano P. G., Musier-Forsyth K. (2007) Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain. Proc. Natl. Acad. Sci. U.S.A. 7, 2127-2132.
34. Vargas-Rodriguez O. and Musier-Forsyth K. (2013) Exclusive use of trans-editing domains prevents proline mistranslation. J. Biol. Chem. 20, 14391–14399.
35. Vecchione J. J. and Sello J. K. (2008) Characterization of an inducible, antibiotic-resistant aminoacyl-tRNA synthetase gene in Streptomyces coelicolor. J. Bacteriol. 18, 6253-6257.
36. Wang C. X., Zhu M. X., Chen X. H. and Qu B. (2011) Review on allelopathy of exotic invasive plants. Procedia Engineering. 18, 240-246.
37. Wong, F.C., Beuning, P.J., Silvers, C., Musier-Forsyth, K. (2003) An isolate class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid. J Biol Chem. 52, 52857-52864.
38. Yadavalli S. S. and Ibba M. (2012) Quality control in aminoacyl-tRNA synthesis: its role in translational fidelity. Adv. Protein Chem. Struct. Biol. 86, 1–43
39. Yanagisawa T, Kawakami M. (2003) How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid? Evidence for two evolutionarily distinct isoleucyl-tRNA synthetases conferring self-defense. J. Biol. Chem. 28, 25887-25894.
40. Yaremchuk A., Cusack S. and Tukalo M. (2000) Crystal structure of a eukaryote/archaeon-like proly-tRNA synthetase and its complex with tRNAPro (CGG). EMBO. J. 17, 4745–4758.
指導教授 王健家(Chien-Chia Wang) 審核日期 2018-7-16
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