Advertisement

Advances in understanding of the oxysterol-binding protein homologous in yeast and filamentous fungi

  • Shangkun Qiu
  • Bin ZengEmail author
Review
  • 2 Downloads

Abstract

Oxysterol-binding protein is an important non-vesicular trafficking protein involved in the transportation of lipids in eukaryotic cells. Oxysterol-binding protein is identified as oxysterol-binding protein-related proteins (ORPs) in mammals and oxysterol-binding protein homologue (Osh) in yeast. Research has described the function and structure of oxysterol-binding protein in mammals and yeast, but little information about the protein’s structure and function in filamentous fungi has been reported. This article focuses on recent advances in the research of Osh proteins in yeast and filamentous fungi, such as Aspergillus oryzae, Aspergillus nidulans, and Candida albicans. Furthermore, we point out some problems in the field, summarizing the membrane contact sites (MCS) of Osh proteins in yeast, and consider the future of Osh protein development.

Keywords

Oxysterol-binding protein homologs Filamentous fungi Yeast Structure and function 

Notes

Acknowledgements

We are grateful to the other staff of this laboratory (Hu Jianwen, Han Jizhong, Sun Yunlong, Li Haoran, Liu Mengmeng, etc.) for their other assistance in this article. The authors thank them for their long-standing support for the author’s scientific work.

Authors’ contributions

Shangkun Qiu mainly participated in the data collection and article design of this article, including content writing, chapter design, and graphic design. Bin Zeng mainly provided technical support and financial assistance.

Funding

This study was financially supported by these projects in China (No.31460447, 31171731, 20142BDH80003, 2013-CXTD002, 3000035402, 00001384, 30000411, 300098020110, 300098030105, “555 talent project” of Jiangxi Province), Jiangxi Province Key Laboratory of Bioprocess Engineering, and Co-Innovation Center for In Vitro Diagnostic Reagents and Devices of Jiangxi Province.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

References

  1. Altmann K, Westermann B (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410–5417.  https://doi.org/10.1091/mbc.e05-07-0678 Google Scholar
  2. Alvarez FJ, Douglas LM, Konopka JB (2007) Sterol-rich plasma membrane domains in fungi. Eukaryot Cell 6(5):755–763.  https://doi.org/10.1128/EC.00008-07 Google Scholar
  3. Barlowe CK, Miller EA (2013) Secretory protein biogenesis and traffic in the early secretory pathway. Genetics 193(2):383–410.  https://doi.org/10.1534/genetics.112.142810 Google Scholar
  4. Beh CT, Cool L, Phillips J, Rine J (2001) Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 157(3):1117–1140Google Scholar
  5. Bosch M, Marí M, Herms A, Fernández A, Fajardo A, Kassan A, Giralt A, Colell A, Balgoma D, Barbero E, González-Moreno E, Matias N, Tebar F, Balsinde J, Camps M, Enrich C, Gross SP, García-Ruiz C, Pérez-Navarro E, Fernández-Checa JC, Pol A (2011) Caveolin-1 deficiency causes cholesterol-dependent mitochondrial dysfunction and apoptotic susceptibility. Curr Biol 21(8):681–686.  https://doi.org/10.1016/j.cub.2011.03.030 Google Scholar
  6. Bühler N, Hagiwara D, Takeshita N (2015) Functional analysis of sterol transporter orthologues in the filamentous fungus Aspergillus nidulans. Eukaryot Cell 14(9):908–921.  https://doi.org/10.1128/EC.00027-15 Google Scholar
  7. Chung J, Torta F, Masai K, Lucast L, Czapla H, Tanner LB, Narayanaswamy P, Wenk MR, Nakatsu F, de Camilli P (2015) PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts. Science 349(6246):428–432.  https://doi.org/10.1126/science.aab1370 Google Scholar
  8. Dawson PA, Van der Westhuyzen DR, Goldstein JL, Brown MS (1989) Purification of oxysterol binding protein from hamster liver cytosol. J Biol Chem 264(15):9046–9052Google Scholar
  9. De Matteis MA, Wilson C, D'Angelo G (2013) Phosphatidylinositol-4-phosphate: the Golgi and beyond. Bioessays 35(7):612–622.  https://doi.org/10.1002/bies.201200180 Google Scholar
  10. Dittman JS, Menon AK (2016) Speed limits for nonvesicular intracellular sterol transport. Trends Biochem Sci 42(2):90–97.  https://doi.org/10.1016/j.tibs.2016.11.004 Google Scholar
  11. Douglas LM, Konopka JB (2016) Plasma membrane organization promotes virulence of the human fungal pathogen Candida albicans. J Microbiol 54(3):178–191.  https://doi.org/10.1007/s12275-016-5621-y Google Scholar
  12. Du X, Kumar J, Ferguson C et al (2011) A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking. J Cell Biol 192(1):121–135.  https://doi.org/10.1083/jcb.201004142 Google Scholar
  13. Du X, Brown AJ, Yang H (2015) Novel mechanisms of intracellular cholesterol transport: oxysterol-binding proteins and membrane contact sites. Curr Opin Cell Biol 35:37–42.  https://doi.org/10.1016/j.ceb.2015.04.002 Google Scholar
  14. Du X, Turner N, Yang H (2017) The role of oxysterol-binding protein and its related proteins in cancer. Semin Cell Dev Biol 81(7):149–153.  https://doi.org/10.1016/j.semcdb.2017.07.017 Google Scholar
  15. Encinar DDJ, Idrissi FZ, Fernandez-Golbano IM et al (2017) ORP-mediated ER contact with endocytic sites facilitates actin polymerization. Dev Cell 43(5):588–602.e6.  https://doi.org/10.1016/j.devcel.2017.10.031 Google Scholar
  16. Escajadillo T, Wang H, Li L, Li D, Sewer MB (2016) Oxysterol-related-binding-protein related Protein-2 (ORP2) regulates cortisol biosynthesis and cholesterol homeostasis. Mol Cell Endocrinol 427:73–85.  https://doi.org/10.1016/j.mce.2016.03.006 Google Scholar
  17. Fernándezbusnadiego R, Saheki Y, De CP (2015) Three-dimensional architecture of extended synaptotagmin-mediated endoplasmic reticulum–plasma membrane contact sites. Proc Natl Acad Sci U S A 112(16):2004–2013.  https://doi.org/10.1073/pnas.1503191112 Google Scholar
  18. Fukuda R, Ohta A (2013) Utilization of hydrophobic substrate by Yarrowia lipolytica. Yarrowia lipolytica :111–119.  https://doi.org/10.1007/978-3-642-38320-5_5
  19. Fukuda R, Ohta A (2017) Enzymes for aerobic degradation of alkanes in yeasts. In: Aerobic Utilization of Hydrocarbons, Oils and Lipids.  https://doi.org/10.1007/978-3-319-39782-5_7-1
  20. Ghai R, Du X, Wang H et al (2017) ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P2) and regulate its level at the plasma membrane. Nat Commun 8(1):757.  https://doi.org/10.1038/s41467-017-00861-5 Google Scholar
  21. Ghugtyal V, Garcia-Rodas R, Seminara A, Schaub S, Bassilana M, Arkowitz RA (2015) Phosphatidylinositol-4-phosphate-dependent membrane traffic is critical for fungal filamentous growth. Proc Natl Acad Sci U S A 112(28):8644.  https://doi.org/10.1073/pnas.1504259112 Google Scholar
  22. Goto A, Liu X, Robinson CA, Ridgway ND (2012) Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis. Mol Biol Cell 23(18):3624–3635.  https://doi.org/10.1091/mbc.E12-04-0283 Google Scholar
  23. Hanada K, Kumagai K, Yasuda S, Miura Y, Kawano M, Fukasawa M, Nishijima M (2003) Molecular machinery for non-vesicular trafficking of ceramide. Nature 426(6968):803–809.  https://doi.org/10.1038/nature02188 Google Scholar
  24. Helle SC, Kanfer G, Kolar K, Lang A, Michel AH, Kornmann B (2013) Organization and function of membrane contact sites. BBA 1833(11):2526–2541.  https://doi.org/10.1016/j.bbamcr.2013.01.028 Google Scholar
  25. Hull CM, Johnson AD (1999) Identification of a mating type-like locus in the asexual pathogenic yeast Candida albicans. Science 285(5431):1271–1275.  https://doi.org/10.1126/science.285.5431.1271 Google Scholar
  26. Im YJ, Raychaudhuri S, Prinz WA, Hurley JH (2005) Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437(7055):154–158.  https://doi.org/10.1038/nature03923 Google Scholar
  27. Iwama R, Kobayashi S, Ohta A, Horiuchi H, Fukuda R (2014) Fatty aldehyde dehydrogenase multigene family involved in the assimilation of n-alkanes in Yarrowia lipolytica. J Biol Chem 289(48):33275–33286.  https://doi.org/10.1074/jbc.M114.596890 Google Scholar
  28. Iwama R, Kobayashi S, Ohta A, Horiuchi H, Fukuda R (2015) Alcohol dehydrogenases and an alcohol oxidase involved in the assimilation of exogenous fatty alcohols in Yarrowia lipolytica. FEMS Yeast Res 15(3):fov014.  https://doi.org/10.1093/femsyr/fov014 Google Scholar
  29. Iwama R, Kobayashi S, Ishimaru C, Ohta A, Horiuchi H, Fukuda R (2016) Functional roles and substrate specificities of twelve cytochromes P450 belonging to CYP52 family in n -alkane assimilating yeast Yarrowia lipolytica. Fungal Genet Biol 91:43–54.  https://doi.org/10.1016/j.fgb.2016.03.007 Google Scholar
  30. Iwama R, Hara M, Mizuike A, Horiuchi H, Fukuda R (2018) Osh6p, a homologue of the oxysterol-binding protein, is involved in production of functional cytochrome P450 belonging to CYP52 family in n-alkane-assimilating yeast Yarrowia lipolytica. Biochem Biophys Res Commun 499(4):836–842.  https://doi.org/10.1016/j.bbrc.2018.04.002 Google Scholar
  31. Johansson M, Bocher V, Lehto M, Chinetti G, Kuismanen E, Ehnholm C, Staels B, Olkkonen VM (2003) The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct. Mol Biol Cell 14(3):903–915.  https://doi.org/10.1091/mbc.e02-08-0459 Google Scholar
  32. Johansson M, Lehto M, Tanhuanpã ÃK, Cover TL, Olkkonen VM (2005) The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol Biol Cell 16(12):5480–5492.  https://doi.org/10.1091/mbc.e05-03-0189 Google Scholar
  33. Keller P, Simons K (1997) Post-Golgi biosynthetic trafficking. J Cell Sci 110(Pt 24):3001Google Scholar
  34. Kentala H, Weber-Boyvat M, Olkkonen VM (2015) OSBP-related protein family: mediators of lipid transport and signaling at membrane contact sites. Int Rev Cell Mol Biol 321:299–340.  https://doi.org/10.1016/bs.ircmb.2015.09.006 Google Scholar
  35. Kulak NA, Pichler G, Paron I, Nagaraj N, Mann M (2014) Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nat Methods 11(3):319–324.  https://doi.org/10.1038/nmeth.2834 Google Scholar
  36. Kullberg BJ, Arendrup MC (2015) Invasive candidiasis. N Engl J Med 373(15):1445–1456.  https://doi.org/10.1056/NEJMra1315399 Google Scholar
  37. Li JW, Xiao YL, Lai CF, Lou N, Ma HL, Zhu BY, Zhong WB, Yan DG (2016) Oxysterol-binding protein-related protein 4L promotes cell proliferation by sustaining intracellular Ca2+ homeostasis in cervical carcinoma cell lines. Oncotarget 7(40):65849–65861.  https://doi.org/10.18632/oncotarget.11671 Google Scholar
  38. Maeda K, Anand K, Chiapparino A, Kumar A, Poletto M, Kaksonen M, Gavin AC (2013) Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 501(7466):257–261.  https://doi.org/10.1038/nature12430 Google Scholar
  39. Manik MK, Yang H, Tong J, Im YJ (2017) Structure of yeast OSBP-related protein Osh1 reveals key determinants for lipid transport and protein targeting at the nucleus-vacuole junction. Structure 25(4):617–629.  https://doi.org/10.1016/j.str.2017.02.010 Google Scholar
  40. Martin LA, Kennedy BE, Karten B (2016) Mitochondrial cholesterol: mechanisms of import and effects on mitochondrial function. J Bioenerg Biomembr 48(2):137–151.  https://doi.org/10.1007/s10863-014-9592-6 Google Scholar
  41. Mccaffrey LM, Macara IG (2011) Epithelial organization, cell polarity and tumorigenesis. Trends Cell Biol 21(12):727–735.  https://doi.org/10.1016/j.tcb.2011.06.005 Google Scholar
  42. Mesmin B, Bigay J, Moser von Filseck J, Lacas Gervais S, Drin G, Antonny B (2013) A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP. Cell 155(4):830–843.  https://doi.org/10.1016/j.cell.2013.09.056 Google Scholar
  43. Mesmin B, Bigay J, Polidori J, Jamecna D, Lacas-Gervais S, Antonny B (2017) Sterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP. EMBO J 36(21):3156–3174.  https://doi.org/10.15252/embj.201796687 Google Scholar
  44. Mizunoyamasaki E, Medkova M, Coleman J, Novick P (2010) Phosphatidylinositol 4-phosphate controls both membrane recruitment and a regulatory switch of the Rab GEF Sec2p. Dev Cell 18(5):828–840.  https://doi.org/10.1016/j.devcel.2010.03.016 Google Scholar
  45. Nicaud JM (2012) Yarrowia lipolytica. Yeast 29(10):409–418.  https://doi.org/10.1002/yea.2921 Google Scholar
  46. Olkkonen VM (2015) OSBP-related protein family in lipid transport over membrane contact sites. Lipid Insights 8(Suppl 1):1–9.  https://doi.org/10.4137/LPI.S31726 Google Scholar
  47. Olkkonen VM, Li S (2013) Oxysterol-binding proteins: sterol and phosphoinositide sensors coordinating transport, signaling and metabolism. Prog Lipid Res 52(4):529–538.  https://doi.org/10.1016/j.plipres.2013.06.004 Google Scholar
  48. Peretti D, Dahan N, Shimoni E, Hirschberg K, Lev S (2008) Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol Biol Cell 19(9):3871–3884.  https://doi.org/10.1091/mbc.e08-05-0498 Google Scholar
  49. Phillips MJ, Voeltz GK (2016) Structure and function of ER membrane contact sites with other organelles. Nat Rev Mol Cell Biol 17(2):69–82.  https://doi.org/10.1038/nrm.2015.8 Google Scholar
  50. Prinz WA (2014) Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics. Cell Biol 205(6):759–769.  https://doi.org/10.1083/jcb.201401126 Google Scholar
  51. Quon E, Sere YY, Chauhan N, Johansen J, Sullivan DP, Dittman JS, Rice WJ, Chan RB, di Paolo G, Beh CT, Menon AK (2018) Endoplasmic reticulum-plasma membrane contact sites integrate sterol and phospholipid regulation. PLoS Biol 16(5):e2003864.  https://doi.org/10.1371/journal.pbio.2003864 Google Scholar
  52. Raychaudhuri S, Prinz WA (2011) The diverse functions of oxysterol-binding proteins. Annu Rev Cell Dev Biol 26(1):157–177.  https://doi.org/10.1146/annurev.cellbio.042308.113334 Google Scholar
  53. Rockenfeller P, Gourlay CW (2018) Lipotoxicty in yeast: a focus on plasma membrane signalling and membrane contact sites. FEMS Yeast Res 18(4).  https://doi.org/10.1093/femsyr/foy034
  54. Santiago Tirado FH, Legesse Miller A, Schott D, Bretscher A (2011) PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast. Dev Cell 20(1):47–59.  https://doi.org/10.1016/j.devcel.2010.11.006 Google Scholar
  55. Santiagotirado FH, Bretscher A (2011) Membrane-trafficking sorting hubs: cooperation between PI4P and small GTPases at the trans-Golgi network. Trends Cell Biol 21(9):515–525.  https://doi.org/10.1016/j.tcb.2011.05.005 Google Scholar
  56. Schulz TA, Prinz WA (2007) Sterol transport in yeast and the oxysterol binding protein homologue (OSH) family. Biochim Biophys Acta 1771(6):0–780.  https://doi.org/10.1016/j.bbalip.2007.03.003 Google Scholar
  57. Schulz TA, Choi MG, Raychaudhuri S, Mears JA, Ghirlando R, Hinshaw JE, Prinz WA (2009) Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues. J Cell Biol 187(6):889–903.  https://doi.org/10.1083/jcb.200905007 Google Scholar
  58. Smindak RJ, Heckle LA, Chittari SS, Hand MA, Hyatt DM, Mantus GE, Sanfelippo WA, Kozminski KG (2017) Lipid-dependent regulation of exocytosis in S. cerevisiae by OSBP homologue (Osh)4. J Cell Sci 130(22):3891–3906.  https://doi.org/10.1242/jcs.205435 Google Scholar
  59. Soffientini U, Graham A (2016) Intracellular cholesterol transport proteins: roles in health and disease. Clin Sci 130(21):1843–1859.  https://doi.org/10.1042/CS20160339 Google Scholar
  60. Storey MK, Byers DM, Cook HW, Ridgway ND (1998) Cholesterol regulates oxysterol binding protein (OSBP) phosphorylation and Golgi localization in Chinese hamster ovary cells: correlation with stimulation of sphingomyelin synthesis by 25-hydroxycholesterol. Biochem J 336(Pt 1):247–256.  https://doi.org/10.1042/bj3360247 Google Scholar
  61. Strahl T, Thorner J (2007) Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae. BBA 1771(3):353–404.  https://doi.org/10.1016/j.bbalip.2007.01.015 Google Scholar
  62. Strating JRPM, Linden LVD, Albulescu L et al (2015) Itraconazole inhibits enterovirus replication by targeting the oxysterol-binding protein. Cell Rep 10(4):600–615.  https://doi.org/10.1016/j.celrep.2014.12.054 Google Scholar
  63. Szentpetery Z, Várnai P, Balla T (2010) Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling. Proc Natl Acad Sci U S A 107(18):8225–8230.  https://doi.org/10.1073/pnas.1000157107 Google Scholar
  64. Takeshita N, Higashitsuji Y, Konzack S, Fischer R (2008) Apical sterol-rich membranes are essential for localizing cell end markers that determine growth directionality in the filamentous fungus aspergillus nidulans. Mol Biol Cell 19(1):339–351.  https://doi.org/10.1091/mbc.e07-06-0523 Google Scholar
  65. Taylor FR, Kandutsch AA (1985) Oxysterol binding protein. Chem Phys Lipids 38(1):187–194.  https://doi.org/10.1016/0009-3084(85)90066-0 Google Scholar
  66. Taylor FR, Shown EP, Thompson EB et al (1989) Purification, subunit structure, and DNA binding properties of the mouse oxysterol receptor. J Biol Chem 264(31):18433Google Scholar
  67. Tenagy, Park JS, Iwama R, Kobayashi S, Ohta A, Horiuchi H, Fukuda R (2015) Involvement of acyl-CoA synthetase genes in n-alkane assimilation and fatty acid utilization in yeast Yarrowia lipolytica. FEMS Yeast Res 15(4):fov031.  https://doi.org/10.1093/femsyr/fov031 Google Scholar
  68. Tian S, Ohta A, Horiuchi H, Fukuda R (2015) Evaluation of sterol transport from the endoplasmic reticulum to mitochondria using mitochondrially targeted bacterial sterol acyltransferase in Saccharomyces cerevisiae. J Agric Chem Soc Jpn 79(10):1608–1614.  https://doi.org/10.1080/09168451.2015.1058702 Google Scholar
  69. Tian S, Ohta A, Horiuchi H, Fukuda R (2018) Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast. J Biol Chem 293.15(2018):5636–5648.  https://doi.org/10.1074/jbc.RA117.000596
  70. Tong J, Yang H, Ha S, Lee Y, Eom SH, Im YJ (2001) Crystallization and preliminary X-ray crystallographic analysis of the oxysterol-binding protein Osh3 from. Acta Crystallogr 68(12):1498–1502.  https://doi.org/10.1107/S1744309112042510 Google Scholar
  71. Tong J, Yang H, Yang H, Eom SH, Im YJ (2013) Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins. Structure 21(7):1203–1213.  https://doi.org/10.1016/j.str.2013.05.007 Google Scholar
  72. Tong J, Manik MK, Yang H, Im YJ (2016) Structural insights into nonvesicular lipid transport by the oxysterol binding protein homologue family. BBA 1861(8):928–939.  https://doi.org/10.1016/j.bbalip.2016.01.008 Google Scholar
  73. Van EM (2014) ATP-binding cassette transporter A1: key player in cardiovascular and metabolic disease at local and systemic level. Curr Opin Lipidol 25(4):297–303.  https://doi.org/10.1097/MOL.0000000000000088 Google Scholar
  74. Van der Kant R, Fish A, Janssen L et al (2013) Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L. J Cell Sci 126(15):3462–3474.  https://doi.org/10.1242/jcs.129270 Google Scholar
  75. Vihervaara T, Jansen M, Uronen RL, Ohsaki Y, Ikonen E, Olkkonen VM (2011) Cytoplasmic oxysterol-binding proteins: sterol sensors or transporters? Chem Phys Lipids 164(6):443–450.  https://doi.org/10.1016/j.chemphyslip.2011.03.002 Google Scholar
  76. Vipond R, Bricknell IR, Durant E, Bowden TJ, Ellis AE, Smith M, MacIntyre S (1998) Defined deletion mutants demonstrate that the major secreted toxins are not essential for the virulence of Aeromonas salmonicida. Infect Immun 66(5):1990Google Scholar
  77. Von Filseck JM, Mesmin B, Bigay J, Antonny B, Drin G (2014) Building lipid ‘PIPelines’ throughout the cell by ORP/Osh proteins. Biochem Soc Trans 42(5):1465–1470.  https://doi.org/10.1042/BST20140143 Google Scholar
  78. Wirtz KW, Zilversmit DB (1968) Exchange of phospholipids between liver mitochondria and microsomes in vitro. J Biol Chem 243(13):3596–3602Google Scholar
  79. Wong LH, Copic A, Levine TP (2017) Advances on the transfer of lipids by lipid transfer proteins. Trends Biochem Sci 42(7):516–530.  https://doi.org/10.1016/j.tibs.2017.05.001 Google Scholar
  80. Xu X, Bittman R, Duportail G, Heissler D, Vilcheze C, London E (2001) Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts) comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceram. J Biol Chem 276(36):33540–33546.  https://doi.org/10.1074/jbc.M104776200 Google Scholar
  81. Zhang X, Liu L, Jianwen H, Chen F, Zeng B (2017) Recombinant expression and purification of an Oxysterol Binding Protein from Aspergillus oryzae 3.042. BIO Web Conf 8:03006.  https://doi.org/10.1051/bioconf/20170803006 Google Scholar

Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.Jiangxi Province Key Laboratory Bioprocess EngineeringJiangxi Science and Technology Normal UniversityNanchangChina

Personalised recommendations