[an error occurred while processing this directive]
en

Analysis of the aminoacyl-tRNA synthetase genes of silkworm (Bombyx mori)

Expand
  • 1. Medical College of Soochow University, Suzhou 215123, China; 2. National Engineering Laboratory for Modern Silk Soochow University, Suzhou 215123, China

Received date: 2009-04-27

  Revised date: 2009-07-12

  Online published: 2009-12-10

Abstract

For further research on number, type, composition and origin of Bombyx mori aminoacyl-tRNA synthetase (BmaaRS) genes, in silico cloning was performed with Bombyx mori genomic and EST databases. There might be two different sets of aaRS nuclear gene in Bombxy nori genome, which encode mitochondrial BmaaRS and cytoplasmic BmaaRS, respectively. Among BmaaRS genes, there were 2 genes encoding mitochondrial BmSerRS, but no genes encoding cytoplasmic BmHisRS and mitochondrial BmGlnRS, BmLysRS, BmGlyRS, and BmThrRS. The functions of these absent genes could be directly replaced by other proteins with similar functions, or might undergo their distinct BmaaRS functions based on the alternative splice of one certain BmaaRS mRNA. Evidence of EST indicated that BmaaRS performed different alternative splicing patterns. The homology comparison and advanced structural analysis of BmaaRS demonstrated the existence of extended domains of BmaaRS. This is because some different BmaaRSs contained similar domain. Moreover, BmaaRSs with similar functions possessed the similar tertiary structure. Phylogenetic analysis revealed that BmaaRS encoded by two various sources of BmaaRS genes. Mitochondrial and cytoplasmic BmaaRS had different origin.

Cite this article

CAO An-Li, XUE Ren-Yu, SHU Huo-Xiong, WEI Yo-Gong, GONG Cheng-Liang . Analysis of the aminoacyl-tRNA synthetase genes of silkworm (Bombyx mori)[J]. Hereditas(Beijing), 2009 , 31(12) : 1248 -1258 . DOI: 10.3724/SP.J.1005.2009.01248

References

[1] Martinis SA, Plateau P, Cavarelli J, Florentz C. Aminoa-cyl-tRNA synthetases: a family of expanding functions. EMBO J, 1999, 18(17): 4591-4596.

[2] 贾捷, 金由辛. 氨酰tRNA合成酶的分子网络和功能. 生物化学与生物物理进展, 2004, 31(4): 291-295.

[3] Andreoli C, Prokisch H, Hörtnagel K, Mueller JC, Mün-sterkötter M, Scharfe C, Meitinger T. MitoP2, an inte-grated database on mitochondrial proteins in yeast and man. Nucleic Acids Res, 2004, 32: D459-D462.

[4] Hengartner MO. The biochemistry of apoptosis. Nature, 2000, 407(6805): 770-776.

[5] Taylor RW, Turnbull DM. Mitochondrial DNA mutations in human disease. Nat Rev Genet, 2005, 6(5): 389-402.

[6] 周小龙, 王恩多. 与人类疾病相关的几种线粒体氨基酰-tRNA合成酶. 生物化学与生物物理进展, 2008, 35(8): 853-858.

[7] Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Parti-tion of tRNA synthetases into two classes based on mutu-ally exclusive sets of sequence motifs. Nature, 1990, 347(6289): 203-206.

[8] Curnow AW, Ibba M, Söll D. tRNA-dependent asparagine formation. Nature, 1996, 382(6592): 589-590.

[9] Ibba M, Söll D. Aminoacyl-tRNA synthesis. Annu Rev Biochem, 2000, 69: 617-650.

[10] Brindefalk B, Viklund J, Larsson D, Thollesson M, Andersson SG. Origin and evolution of the mitochondrial aminoacyl-tRNA synthetases. Mol Biol and Evol, 2007, 24(3): 743-756.

[11] Chang PK, Dignam JD. Primary structure of alanyl-tRNA synthetase and the regulation of its mRNA levels in Bom-byx mori. J Biol Chem, 1990, 265(34): 20898-20906.

[12] Nada S, Chang PK, Dignam JD. Primary structure of the gene for glycyl-tRNA synthetase from Bombyx mori. J Biol Chem, 1993, 268(11): 7660-7667.

[13] Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS- MODEL workspace: A web-based environment for protein structure homology modelling. Bioinformatics, 2006, 22(2): 195-201.

[14] Martinis SA, Plateau P, Cavarelli J, Florentz C. Aminoa-cyl-tRNA synthetases: a new image for a classical family. Biochimie, 1999, 81(7): 683-700.

[15] Chihade JW, Brown JR, Schimmel PR, Ribas De Pouplana L. Origin of mitochondria in relation to evolutionary his-tory of eukaryotic alanyl-tRNA synthetase. Proc Natl Acad Sci USA, 2000, 97(22): 12153-12157.

[16] Ribas de Pouplana L, Schimmel P. A view into the origin of life: aminoacyl-tRNA synthetases. Cell Mol Life Sci, 2000, 57(6): 865-870.

[17] Hashimoto T, Sánchez LB, Shirakura T, Müller M, Hase-gawa M. Secondary absence of mitochondria in Giardia lamblia and Trichomonas vaginalis revealed by va-lyl-tRNA synthetase phylogeny. Proc Natl Acad Sci USA, 1998, 95(12): 6860-6865.

[18] 林军, 黄京飞. 氨酰tRNA合成酶专一性识别的进化. 生物化学与生物物理进展, 2002, 29(6): 837-841.

[19] Tolkunova E, Park H, Xia J, King MP, Davidson E. The human lysyl-tRNA synthetase gene encodes both the cy-toplasmic and mitochondrial enzymes by means of an un-usual alternative splicing of the primary transcript. J Biol Chem, 2000, 275(45): 35063-35069.

[20] Natsoulis G, Hilger F, Fink GR. The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine tRNA synthetases of S. cerevisiae. Cell, 1986, 46(2): 235-243.

[21] Shiba K, Motegi H, Yoshida M, Noda T. Human aspa-rainyl-tRNA synthetase: molecular cloning and the infer-ence of the evolutionary history of Asx-tRNA synthetase family. Nucleic Acids Res, 1998, 26(22): 5045-5051.

[22] Brown JR, Doolittle WF. Gene descent, duplication, and horizontal transfer in the evolution of glutamyl- and gltaminyl-tRNA synthetases. J Mol Evol, 1999, 49(4): 485-495.

[23] Woese CR, Olsen GJ, Ibba M, Söll D. Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol Mol Biol Rev, 2000, 64(1): 202–236.

[24] Kim S, Lee SW, Choi EC, Choi SY. Aminoacyl

Outlines

/