家蚕氨酰-tRNA合成酶基因分析
收稿日期: 2009-04-27
修回日期: 2009-07-12
网络出版日期: 2009-12-10
基金资助
国家高技术研究发展计划项目(863计划) (编号:2006AA10A118)和国家自然科学基金项目(编号:30671590)资助
Analysis of the aminoacyl-tRNA synthetase genes of silkworm (Bombyx mori)
Received date: 2009-04-27
Revised date: 2009-07-12
Online published: 2009-12-10
为了探讨家蚕氨酰-tRNA合成酶(BmaaRS)基因的数目、种类、结构及起源, 利用家蚕基因组数据和EST数据进行了BmaaRS基因的电子克隆, 结果表明, 家蚕核基因组中含有2套不同的aaRS核基因, 分别编码线粒体和细胞质BmaaRS, 但编码线粒体BmSerRS的基因有2个, 可能缺少编码细胞质的BmHisRS基因和编码线粒体的BmGlnRS、BmLysRS、BmGlyRS和BmThrRS基因, 这些基因的功能可能由具有相似功能的其他蛋白完成, 或通过某个BmaaRS基因的可变剪接分别形成不同功能的BmaaRS。EST证据表明, BmaaRS基因存在不同形式的可变剪接; BmaaRS氨基酸序列的相似性及二、三级结构分析表明部分BmaaRS存在结构域的扩增, 有些不同的BmaaRS具有相同结构域, 相同功能的BmaaRS具有相似的三级结构; 进化分析表明, BmaaRS为2套不同来源的BmaaRS基因编码, 细胞质和线粒体BmaaRS的起源不同。
关键词: 家蚕; 氨酰-tRNA合成酶; 核基因; 线粒体; 电子克隆
曹广力,薛仁宇,朱越雄,魏育红,贡成良 . 家蚕氨酰-tRNA合成酶基因分析[J]. 遗传, 2009 , 31(12) : 1248 -1258 . DOI: 10.3724/SP.J.1005.2009.01248
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.
[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
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