太平洋牡蛎酪氨酸酶基因家族的系统发生分析
收稿日期: 2013-10-28
修回日期: 2013-12-02
网络出版日期: 2014-01-25
基金资助
国家高技术研究发展规划(863计划)项目(编号：2012AA10A405-6)和国家自然科学基金项目(编号：31372524)资助
Phylogenetic analysis of tyrosinase gene family in the Pacific oyster (Crassostrea gigas Thunberg)
Received date: 2013-10-28
Revised date: 2013-12-02
Online published: 2014-01-25
文章利用生物信息学方法对太平洋牡蛎(Crassostrea gigas Thunberg)酪氨酸酶基因家族的氨基酸序列特征、分类及系统发生进行了分析。结果表明, 太平洋牡蛎酪氨酸酶基因家族在进化过程中存在基因扩张现象, 其主要方式是基因重复。太平洋牡蛎酪氨酸酶可分为3种类型：分泌型 (Type A), 胞内型 (Type B)和具跨膜结构域型 (Type C)。根据太平洋牡蛎酪氨酸酶进化树分析, 发现Type A酪氨酸酶中, tyr18与其他Type A酪氨酸酶分化较大, 可能是较早分化出来的酪氨酸酶; Type B酪氨酸中的tyr2和tyr9以及Type C中的tyr8为较早分化出的酪氨酸酶。系统发生树分析发现太平洋牡蛎酪氨酸酶的聚类受酪氨酸酶类型以及基因位置的影响, 其分泌型酪氨酸酶首先与头足类分泌型酪氨酸酶聚在一起, 然后与线形动物门分泌型酪氨酸酶聚在一起, 与腔肠动物门分泌型酪氨酸酶分化明显。太平洋牡蛎胞内型酪氨酸酶自身分化较大, 总体上与线性动物门、其他软体动物胞内型酪氨酸酶聚为一支, 与扁形动物门、脊索动物门、腔肠动物门胞内型酪氨酸酶分化较大。太平洋牡蛎具跨膜结构域型酪氨酸酶与扁形动物门、环形动物门以及脊索动物门具跨膜结构域型酪氨酸酶分化明显, 与合浦珠母贝具跨膜结构域型酪氨酸酶聚为一支。这表明双壳类的Type C型酪氨酸酶与其他物种的同源酶的进化差异较大。文章首次探讨了太平洋牡蛎酪氨酸酶家族分类、分化及系统发生, 以期对太平洋牡蛎酪氨酸酶基因家族的理论研究和实际应用提供依据。
于雪, 于红, 孔令锋, 李琪 . 太平洋牡蛎酪氨酸酶基因家族的系统发生分析[J]. 遗传, 2014 , 36(2) : 135 -144 . DOI: 10.3724/SP.J.1005.2014.0135
The deduced amino acid sequence characteristics, classification and phylogeny of tyrosinase gene family in the Pacific oyster (Crassostrea gigas Thunberg) were analyzed using bioinformatics methods. The results showed that gene duplication was the major cause of tyrosinase gene expansion in the Pacific oyster. The tyrosinase gene family in the Pacific oyster can be further classified into three types: secreted form (Type A), cytosolic form (Type B) and membrane-bound form (Type C). Based on the topology of the phylogenetic tree of the Pacific oyster tyrosinases, among Type A isoforms, tyr18 seemed divergent from other Type A tyrosinases early, while tyr2 and tyr9 appeared divergent early in Type B. In Type C tyrosinses, tyr8 was divergent early. The cluster of the Pacific oyster tyrosinasesis determined by their classifications and positions in the scaffolds. Further analysis suggested that Type A tyrosinases of C. gigas clustered with those from cephalopods and then with nematodes and cnidarians. Type B tyrosinases were generally clustered with the same type of tyrosinases from molluscas and nematodes, and then with those from platyhelminths, cnidarians and chordates. Type A tyrosinases in the Pacific oyster and the Pearl oyster expanded independently and were divergent from membrane-bound form of tyrosinases in chordata, platyhelminthes and annelida. These observations suggested that Type C tyrosinases in the bivalve had a distinct evolution direction.
Key words： Crassostrea gigas; tyrosinase; classification; phylogeny
[1] Ito S, Wakamatsu K, Ozeki H. Chemical analysis of mela-nins and its application to the study of the regulation of melanogenesis. Pigm Cell Res, 2000, 13(Suppl 8): 103– 109. <\p>
[2] Esposito R, D’Aniello S, Squarzoni P, Pezzotti MR, Ris-toratore F, Spagnuolo A. New insights into the evolution of Metazoan tyrosinase gene family. PLoS ONE, 2012, 7(4): E35731. <\p>
[3] Goding GR. Melanocytes: the new black. Int J Biochem Cell Biol, 2007, 39(2): 275–279. <\p>
[4] Gillespie JP, Kanost MR, Trenczek T. Biological mediators ofinsect immunity. Ann Rev Entool, 1997, 42: 611–643. <\p>
[5] Luna-Acosta A, Thomas-Guyon H, Amari M, Rosenfeld E, Bustamante P, Fruitier-Arnaudin I. Differential tissue dis-tribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas. CompBiochemPhysi, 2011, 159B: 220–226. <\p>
[6] Sugumaran M. Unified mechanism for sclerotization of insect cuticle. Adv Insect Physiol, 1998, 27: 229–334. <\p>
[7] Sugumaran M. Molecular mechanisms for mammalian melanogenesis comparison with insect cuticular sclerotiza-tion (minireview). FEBS Lett, 1991, 293(1?2): 4–10. <\p>
[8] Kouhei N, Masato Y, Koichi M, Hiroshi M. Tyrosinase localization in mollusc shells. Comp Biochem Physio B Biochem Mol Biol, 2007, 146: 207–214. <\p>
[9] Zhang C, Xie LP, Huang J, Chen L, Zhang RQ. A novel putative tyrosinase involved in periostracum formation from the pearl oyster (Pinctada fucata). BiochemBiopyhs Res Commun, 2006, 342(2): 632–639. <\p>
[10] Zhou Z, Ni DJ, Wang MQ, Wang LL, Shi XW, Yue F, Liu R, Song LS. The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri. Fish Shellfish Immunology, 2012, 33(2): 375–381. <\p>
[11] Zhang G, Fang X, Guo X, Li L, Luo R, Xu F, Yang P, Zhang L, Wang X, Qi H, Xiong Z, Que H, Xie Y, Holland PW, Paps J, Zhu Y, Wu F, Chen Y, Wang J, Peng C, Meng J, Yang L, Liu J, Wen B, Zhang N, Huang Z, Zhu Q, Feng Y, Mount A, Hedgecock D, Xu Z, Liu Y, Domazet-Loso T, Du Y, Sun X, Zhang S, Liu B, Cheng P, Jiang X, Li J, Fan D, Wang W, Fu W, Wang T, Wang B, Zhang J, Peng Z, Li Y, Li N, Wang J, Chen M, He Y, Tan F, Song X, Zheng Q, Huang R, Yang H, Du X, Chen L, Yang M, Gaffney PM, Wang S, Luo L, She Z, Ming Y, Huang W, Zhang S, Huang B, Zhang Y, Qu T, Ni P, Miao G, Wang J, Wang Q, Steinberg CE, Wang H, Li N, Qian L, Zhang G, Li Y, Yang H, Liu X, Wang J, Yin Y, Wang J. The oyster genome reveals stress adaptation and complexity of shell formation. Nature, 2012, 490: 49–54. <\p>
[12] Cong R, Sun W, Liu G, Fan T, Meng X, Yang L, Zhu L. Purification and characterization of phenoloxidase from clam Ruditapes philippinarum. Fish Shellfish Immunol, 2005, 18(1): 61–70. <\p>
[13] Jiang JW, Xing J, Sheng XZ, Zhan WB. Characterization of phenoloxidase from the bay scallop Argopecten irradians. J Shellfish Res, 2011, 30(2): 273–277. <\p>
[14] Aladaileh S, Rodney P, Nair SV, Raftos DA. Characterization of phenoloxidase activity in Sydney rock oysters (Saccostrea glomerata). CompBiochemPhysiol, 2007, 148(4): 470–480. <\p>
[15] Luna-Gonza´leza A, Maeda-Martíneza AN, Vargas-Alboresb F, Ascencio-Vallea F, Robles-Mungaraya M. Phenoloxidase activity in larval and juvenile homogenates and adult plasma and haemocytes of bivalve molluscs. Fish Shellfish Immunol, 2003, 15(4): 275–282. <\p>
[16] Aguilera F, McDougall C, Degnan MB. Origin, evolution and classification of type-3 copper proteins: lineage-specific gene expansions and losses across the Metazoa. BMC Evol Biol, 2013, 13: 96. <\p>
[17] Petersen TN, Brunak S, Von Heijne G, Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Meth, 2011, 8(10): 785–786. <\p>
/
| 〈 |
|
〉 |
www.chinagene.cn
备案号：京ICP备09063187号-4
总访问:,今日访问:,当前在线:
