Abstract:Bioinformatics research about the WD40 domain contained protein family of Cryptosporidium parvum was conduct in this study, and then structure analysis of the WD40 domain and its function prediction would provide some basic theory for Cryptosporidium parvum gene function studies. Firstly, based on the data collection, we acquired WD40 domain contained protein family's sequences. Then the CDD domain search and alignment analysis were conducted through the NCBI for every protein to ensure that all of them were WD40 domain contained proteins. Lastly, we processed the domain analysis and functional prediction. So, we obtained 50 domain contained proteins of C. parvum Iowa II, and found that there were significant differences among their amino acid sequence length, molecular weight, isoelectric point, etc. And from domain analysis, cgd1_1930, cgd5_740 and cgd4_3360 contains CAF1C_bd super family, which may be involved in DNA repair and replication; cgd4_260 contains ACE1-Sec16-like super family, which may be involved in vesicle formation and material transport; cgd1_2600 contains TAF5_NTD2 domain, which may involved in protein-protein interactions. It's suggested that the WD40 protein family may not only play a role in the interaction alone, but also exert their biological effects through it.
陈川,荆春霞,张鲍欢,张丽菊,黄伟煌,井立鹏,东方,杨光. 基于生物信息学分析微小隐孢子虫含WD40结构域的蛋白功能[J]. 中国人兽共患病学报, 2014, 30(6): 583-587.
CHEN Chuan,JING Chun-xia,ZHANG Bao-huan,ZHANG Li-ju,HUANG Wei-huang,JING Li-peng,DONG Fang, YANG Guang. Function of proteins with WD40 domain in Cryptosporidium parvum based on bioinformatics. Chinese Journal of Zoonoses, 2014, 30(6): 583-587.
[1]O’Donoghue PJ. Cryptosporidium and cryptosporidiosis in man and animals[J]. Int J Parasitol, 1995, 25(2): 139-195. [2]Abrahamsen MS, Templeton TJ, Enomoto S, et al. Complete genome sequence of the apicomplexan, Cryptosporidium parvum[J]. Science, 2004, 304(5669): 441-445. [3]Xu P, Widmer G, Wang Y, et al. The genome of Cryptosporidium hominis[J]. Nature, 2004, 431(7012): 1107-1112. [4]Colford JM Jr, Tager IB, Hirozawa AM, et al. Cryptosporidiosis among patients infected with human immunodeficiency virus. Factors related to symptomatic infection and survival[J]. Am J Epidemiol, 1996, 144(9): 807-816. [5]Simon MI, Strathmann MP, Gautam N. Diversity of G proteins in signal transduction[J]. Science, 1991, 252(5007): 802-808. [6]Xu C, Min J. Structure and function of WD40 domain proteins[J]. Protein Cell, 2011, 2(3): 202-214. DOI: 10.1007/s13238-011-1018-1 [7]Braaten D, Luban J. Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells[J]. EMBO J, 2001, 20(6): 1300-1309. [8]Li D, Roberts R. WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases[J]. Cell Mol Life Sci, 2001, 58(14): 2085-2097. [9]Cao R, Zhang Y. The functions of E (Z)/EZH2-mediated methylation of lysine 27 in histone H3[J]. Curr Opin Genet Dev, 2004, 14(2): 155-164. [10]Feng Q, Zhang Y. The NuRD complex: linking histone modification to nucleosome remodeling[J]. Curr Top Microbiol Immunol, 2003, 274: 269-290. [11]Thornton C, Tang KC, Phamluong K, et al. Spatial and temporal regulation of RACK1 function and N-methyl-D-aspartate receptor activity through WD40 motif-mediated dimerization[J]. J Biol Chem, 2004, 279(30): 31357-31364. [12]Murzina NV, Pei XY, Zhang W, et al. Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46[J]. Structure, 2008, 16(7): 1077-1085. DOI: 10.1016/j.str.2008.05.006 [13]Song JJ, Garlick JD, Kingston RE. Structural basis of histone H4 recognition by p55[J]. Genes Dev, 2008, 22(10): 1313-1318. DOI: 10.1101/gad.1653308 [14]Lejon S, Thong SY, Murthy A, et al. Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48 FOG-1 complex[J]. J Biol Chem, 2011, 286(2): 1196-1203. DOI: 10.1074/jbc.M110.195842 [15]Gao Z, Huang Z, Olivey HE, et al. FOG-1-mediated recruitment of NuRD is required for cell lineage re-enforcement during haematopoiesis[J]. EMBO J, 2010, 29(2):457-468. DOI: 10.1038/emboj.2009.368 [16]Whittle JR, Schwartz TU. Structure of the Sec13-Sec16 edge element,a template for assembly of the COPII vesicle coat[J]. J Cell Biol,2010,190(3):347-361. DOI:10.1083/jcb.201003092 [17]Marchler-Bauer A, Lu S, Anderson JB, et al. CDD: a Conserved Domain Database for the functional annotation of proteins[J]. Nucleic Acids Res, 2011, 39(D): 225-229. DOI: 10.1093/nar/gkq1189 [18]Mitsuzawa H, Seino H, Yamao F, et al. Two WD repeat-containing TAFs in fission yeast that suppress defects in the anaphase-promoting complex[J]. J Biol Chem, 2001, 276(20): 17117-17124. [19]Madej T, Addess KJ, Fong JH, et al. MMDB: 3D structures and macromolecular interactions[J]. Nucleic Acids Res, 2012, 40(D): 461-464. DOI: 10.1093/nar/gkr1162 [20]Fong HK, Hurley JB, Hopkins RS, et al. Repetitive segmental structure of the transducin β subunit: Homology with the CDC4 gene and identification of related mRNAs[J]. Proc Natl Acad Sci USA, 1986, 83(7): 2162-2166. [21]Paoli M. Protein folds propelled by diversity[J]. Pro Biophys Mol Biol, 2001, 76(1/2): 103-130. [22]Smith TF, Gaitatzes C, Saxena K, et al. The WD repeat: a common architecture for diverse functions[J]. Trends Biochem Sci, 1999, 24(5): 181-185. [23]Tyers M, Willems AR. One ring to rule a superfamily of E3 ubiquitin ligases[J]. Science, 1999, 284(5414): 603-604. [24]Ramsay NA, Glover BJ. MYB-bHLH-WD40 protein complex and the evolution of cellular diversity[J]. Trends Plant Sci, 2005, 10(2): 63-70. [25]Dell EJ, Connor J, Chen S, et al. The betagamma subunit of heterotrimeric G proteins interacts with RACK1 and two other WD repeat proteins[J]. J Biol Chem, 2002, 277(51): 49888-49895.