PDF下载 分享
[1]贺双意,孔佳,王媚媚,等.人、猪和鸡源SAMHD1蛋白的酶活性研究[J].天津大学学报(自然科学版),2018,(01):9-17.[doi:10.11784/tdxbz201703051]
 He Shuangyi,Kong Jia,Wang Meimei,et al.Enzymatic Activities of SAMHD1s from Human, Pig,and Chicken[J].Journal of Tianjin University,2018,(01):9-17.[doi:10.11784/tdxbz201703051]
点击复制

人、猪和鸡源SAMHD1蛋白的酶活性研究

参考文献/References:

[1] Kim C A, Gingery M, Pilpa R M, et al. The SAM domain of polyhomeotic forms a helical polymer[J]. Nat Struct Biol, 2002, 9(6):453-457.
[2] Green J B, Gardner C D, Wharton R P, et al. RNA recognition via the SAM domain of Smaug[J]. Molecular Cell, 2003, 11(6):1537-1548.
[3] Qiao F, Bowie J U. The many faces of SAM[J]. Sci STKE, 2005, 3(1):286-295.
[4] Oussenko I A, Sanchez R, Bechhofer D H. Bacillus subtilis YhaM, a member of a new family of 3’-to-5’ exonucleases in gram-positive bacteria[J]. Journal of Bacteriology, 2002, 184(22):6250-6259.
[5] Sinkunas T, Gasiunas G, Fremaux C, et al. Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the CRISPR/Cas immune system[J]. EMBO J, 2011, 30(7):1335-1342.
[6] Vorontsov II, Minasov G, Kiryukhina O, et al. Characterization of the deoxynucleotide triphosphate triphosphohydrolase(dNTPase)activity of the EF1143 protein from Enterococcus faecalis and crystal structure of the activator-substrate complex[J]. J Biol Chem, 2011, 286(38):33158-33166.
[7] Yang S, Shan T, Zhou Y, et al. Molecular cloning and characterizations of porcine SAMHD1 and its roles in replication of highly pathogenic porcine reproductive and respiratory syndrome virus[J]. Dev Comp Immunol, 2014, 47(2):234-246.
[8] Baldauf H M, Pan X, Erikson E, et al. SAMHD1 restricts HIV-1 infection in resting CD4(+)T cells[J]. Nat Med, 2012, 18(11):1682-1687.
[9] Sommer A F, Riviere L, Qu B, et al. Restrictive influence of SAMHD1 on Hepatitis B virus life cycle[J]. Sci Rep, 2016, 6(1):26616-26629.
[10] Jermy A. Viral infection:SAMHD1 cuts the power to HIV-1[J]. Nat Rev Microbiol, 2012, 10(4):237-245.
[11] Yan J, Kaur S, Delucia M, et al. Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection[J]. J Biol Chem, 2013, 288(15):10406-10417.
[12] Beloglazova N, Flick R, Tchigvintsev A, et al. Nuclease activity of the human SAMHD1 protein implicated in the Aicardi-Goutieres syndrome and HIV-1 restriction[J]. J Biol Chem, 2013, 288(12):8101-8110.
[13] Ryoo J, Choi J, Oh C, et al. The ribonuclease activity of SAMHD1 is required for HIV-1 restriction[J]. Nat Med, 2014, 20(8):936-941.
[14] Tungler V, Staroske W, Kind B, et al. Single-stranded nucleic acids promote SAMHD1 complex formation[J]. J Mol Med(Berl), 2013, 91(6):759-770.
[15] Choi J, Ryoo J, Oh C, et al. SAMHD1 specifically restricts retroviruses through its RNase activity[J]. Retrovirology, 2015, 12(1):46-57.
[16] Arnold L H, Groom H C, Kunzelmann S, et al. Phospho-dependent regulation of SAMHD1 oligomerisation couples catalysis and restriction[J]. PLoS Pathog, 2015, 11(10):1-30.
[17] Tang C, Ji X, Wu L, et al. Impaired dNTPase activity of SAMHD1 by phosphomimetic mutation of Thr-592[J]. J Biol Chem, 2015, 290(44):26352-26359.
[18] Yan J, Hao C, Delucia M, et al. CyclinA2-cyclin-dependent kinase regulates SAMHD1 protein phosphohydrolase domain[J]. J Biol Chem, 2015, 290(21):13279-13292.
[19] Garner M G, Whan I F, Gard G P, et al. The expected economic impact of selected exotic diseases on the pig industry of Australia[J]. Rev Sci Tech, 2001, 20(3):671-685.
[20] Nieuwenhuis N, Duinhof T F, van Nes A. Economic analysis of outbreaks of porcine reproductive and respiratory syndrome virus in nine sow herds[J]. Vet Rec, 2012, 170(9):225.
[21] Neumann E J, Kliebenstein J B, Johnson C D, et al. Assessment of the economic impact of porcine reproductive and respiratory syndrome on swine production in the United States[J]. J Am Vet Med Assoc, 2005, 227(3):385-392.
[22] Cribier A, Descours B, Valadao A L, et al. Phosphorylation of SAMHD1 by cyclin A2/CDK1 regulates its restriction activity toward HIV-1[J]. Cell Rep, 2013, 3(4):1036-1043.
[23] Pauls E, Ruiz A, Badia R, et al. Cell cycle control and HIV-1 susceptibility are linked by CDK6-dependent CDK2 phosphorylation of SAMHD1 in myeloid and lymphoid cells[J]. J Immunol, 2014, 193(4):1988-1997.
[24] Goldstone D C, Ennis-Adeniran V, Hedden J J, et al. HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase[J]. Nature, 2011, 480(7377):379-382.
[25] Li Y, Peng X, Qin X. Recombinant expression, purification, and crystallization of the sterile alpha-motif/histidine-aspartate domain-containing protein from chicken[J]. Protein Expr Purif, 2017, 133(1):96-101.
[26] Ji X, Wu Y, Yan J, et al. Mechanism of allosteric activation of SAMHD1 by dGTP[J]. Nat Struct Mol Biol, 2013, 20(11):1304-1309.
[27] Zhu C, Gao W, Zhao K, et al. Structural insight into
dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolase[J]. Nat Commun, 2013, 4(1):2722-2730.
[28] Hrecka K, Hao C, Gierszewska M, et al. Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein[J]. Nature, 2011, 474(7353):658-661.
[29] Laguette N, Sobhian B, Casartelli N, et al. SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx[J]. Nature, 2011, 474(7353):654-657.
[30] Oberstrass F C, Lee A, Stefl R, et al. Shape-specific recognition in the structure of the Vts1p SAM domain with RNA[J]. Nat Struct Mol Biol, 2006, 13(2):160-167.
[31] Davis A S, Taubenberger J K, Bray M. The use of nonhuman primates in research on seasonal, pandemic and avian influenza, 1893-2014[J]. Antiviral Res, 2015, 117(1):75-98.
[32] Kapgate S S, Barbuddhe S B, Kumanan K. Next generation sequencing technologies:Tool to study avian virus diversity[J]. Acta Virologica, 2015, 59(1):3-13.

备注/Memo

收稿日期: 2017-03-20; 修回日期: 2017-05-19.
作者简介: 贺双意(1990—), 男, 硕士研究生, shyhebio@163.com.
通讯作者: 秦晓红, qinxiaohong@tju.edu.cn.
网络出版时间: 2017-06-13.网络出版地址: http://kns.cnki.net/kcms/detail/12.1127.N.20170613.1052.004.html.
基金项目: 国家自然科学基金资助项目(31400465); 天津市自然科学基金资助项目(15JCQNJC09800); 南开大学药物化学生物学国家重点实验室资助项目(20150629).
Supported by the National Natural Science Foundation of China(No.,31400465), the Natural Science Foundation of Tianjin(No.,15JCQNJC09800) and the State Key Laboratory of Medicinal Chemical Biology(Nankai University)(No.,20150629).

更新日期/Last Update: 2018-01-10