Advances on the Baculovirus Expression Vector System for Protein Complex Production

Abstract

Abstract: Most essential functions of eukaryotic cells are catalyzed by complex built of many subunits. To well understand their biological function in the process of health and disease, it is imperative to study these complexes. The low abundance and heterogeneity of many essential complexes have limited their extraction from native source material. The baculovirus expression vector system（BEVS）, specifically tailored for multiprotein complex production, has been proven itself to be uniquely suited for overcoming this impeding bottleneck. Here we highlight recent major achievements in multiprotein complex structure research which were catalyzed by this versatile recombinant complex expression tool.

Wan Jing, Xiang Xingwei, Jiang Lingli, Zhou Xiangyang,. Advances on the Baculovirus Expression Vector System for Protein Complex Production[J]. Biotechnology Bulletin, 2014, 0(2): 7-14.

References

[1] Bieniossek C, Imasaki T, Takagi Y, et al. MultiBac：expanding the research toolbox for multiprotein complexes[J]. Trends Biochem Sci, 2012, 37：49-57.
[2] Kornberg RD. Mediator and the mechanism of transcriptional activation[J]. Trends Biochem Sci, 2005, 30：235-239.
[3] Boube M, Joulia L, Cribbs DL, et al. Evidence for a mediator of RNA polymerase II transcriptional regulation conserved from yeast to man[J]. Cell, 2002, 110：143-151.
[4] Malik S, Roeder RG. The metazoan Mediator co-activator complex as an integrative hub for transcriptional regulation[J]. Nat Rev Genet, 2010, 11：761-772.
[5] Bjorklund S, Gustafsson CM. The yeast Mediator complex and its regulation[J]. Trends Biochem Sci, 2005, 30：240-244.
[6] Guglielmi B, van Berkum NL, Klapholz B, et al. A high resolution protein interaction map of the yeast Mediator complex[J]. Nucleic Acids Res, 2004, 32：5379-5391.
[7] Firestein R, Bass AJ, Kim SY, et al. CDK8 is a colorectal cancer oncogene that regulates beta-catenin activity[J]. Nature, 2008, 455：547-551.
[8] Rump P, Niessen RC, Verbruggen KT, et al. A novel mutation in MED12 causes FG syndrome（Opitz-Kaveggia syndrome）[J]. Clin Genet, 2011, 79：183-188.
[9] Graham JM Jr, Visootsak J, Dykens E, et al. Behavior of 10 patients with FG syndrome（Opitz-Kaveggia syndrome）and the p.R961W mutation in the MED12 gene[J]. Am J Med Genet A, 2008, 146A：3011-3007.
[10] Makinen N, Mehine M, Tolvanen J, et al. MED12, the mediator complex subunit 12 gene, is mutated at high frequency in uterine leiomyomas[J]. Science, 2011, 334：252-255.
[11] Berti L, Mittler G, Przemeck GK, et al. Isolation and characterization of a novel gene from the DiGeorge chromosomal region that encodes for a mediator subunit[J]. Genomics, 2001, 74：320-332.
[12] Kaufmann R, Straussberg R, Mandel H, et al. Infantile cerebral and cerebellar atrophy is associated with a mutation in the MED17 subunit of the transcription preinitiation mediator complex[J]. Am J Hum Genet, 2010, 87：667-670.
[13] Hashimoto S, Boissel S, Zarhrate M, et al. MED23 mutation links intellectual disability to dysregulation of immediate early gene expression[J]. Science, 2011, 333：1161-1163.
[14] Rieker RJ, Agaimy A, Moskalev EA, et al. Mutation status of the mediator complex subunit 12（MED12）in uterine leiomyomas and concurrent/metachronous multifocal peritoneal smooth muscle nodules（leiomyomatosis peritonealis disseminata）[J]. Pathology, 2013, 45：388-392.
[15] Cai G, Imasaki T, Takagi Y, et al. Mediator structural conservation and implications for the regulation mechanism[J]. Structure, 2009, 17：559-567.
[16] Davis JA, Takagi Y, Kornberg RD, et al. Structure of the yeast RNA polymerase II holoenzyme：Mediator conformation and polymerase interaction[J]. Mol Cell, 2002, 10：409-515.
[17] Conaway RC, Conaway JW. Origins and activity of the mediator complex[J]. Semin Cell Dev Biol, 2011, 22：729-734.
[18] Thompson CM, Koleske AJ, Chao DM, et al. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast[J]. Cell, 1993, 73：1361-1375.
[19] Hengartner CJ, Thompson CM, Zhang J, et al. Association of an activator with an RNA polymerase II holoenzyme[J]. Genes Dev, 1995, 9：897-910.
[20] Lee YC, Park JM, Min S, et al. An activator binding module of yeast RNA polymerase II holoenzyme[J]. Mol Cell Biol, 1999, 19：2967-2976.
[21] Taatjes DJ. The human Mediator complex：a versatile, genome-wide regulator of transcription[J]. Trends Biochem Sci, 2010, 35：315-22.
[22] Balamotis MA, Pennella MA, Stevens JL, et al. Complexity in transcription control at the activation domain-mediator interface[J]. Sci Signal, 2009, 2：ra20.
[23] Koh SS, Ansari AZ, Ptashne M, et al. An activator target in the RNA polymerase II holoenzyme[J]. Mol Cell, 1998, 1：895-904.
[24] Takagi Y, Calero G, Komori H, et al. Head module control of mediator interactions[J]. Mol Cell, 2006, 23：355-364.
[25] Cai G, Imasaki T, Yamada K, et al. Mediator head module structure and functional interactions[J]. Nat Struct Mol Biol, 2010, 17：273-279.
[26] Imasaki T, Calero G, Cai G, et al. Architecture of the Mediator head module[J]. Nature, 2011, 475：240-243.
[27] Pines J. Cubism and the cell cycle：the many faces of the APC/C[J]. Nat Rev Mol Cell Biol, 2011, 12：427-438.
[28] Sullivan M, Morgan DO. Finishing mitosis, one step at a time[J]. Nat Rev Mol Cell Biol, 2007, 8：894-903.
[29] Barford D. Structural insights into anaphase-promoting complex function and mechanism[J]. Philos Trans R Soc Lond B Biol Sci, 2011, 366：3605-3624.
[30] Schreiber A, Stengel F, Zhang Z, et al. Structural basis for the subunit assembly of the anaphase-promoting complex[J]. Nature, 2011, 470：227-232.
[31] Zhang Z, Yang J, Kong EH, et al. Recombinant expression, reconstitution and structure of human anaphase-promoting complex（APC/C）[J]. Biochem J, 2013, 449：365-371.
[32] da Fonseca PC, Kong EH, Zhang Z, et al. Structures of APC/C（Cdh1）with substrates identify Cdh1 and Apc10 as the D-box co-receptor[J]. Nature, 2011, 470：274-278.
[33] Uzunova K, Dye BT, Schutz H, et al. APC15 mediates CDC20 autoubiquitylation by APC/C（MCC）and disassembly of the mitotic checkpoint complex[J]. Nat Struct Mol Biol, 2012, 19：1116-123.
[34] Berger I, Fitzgerald DJ, Richmond TJ. Baculovirus expression system for heterologous multiprotein complexes[J]. Nat Biotechnol, 2004, 22：1583-1587.
[35] Bitinaite J, Rubino M, Varma KH, et al. USER friendly DNA engineering and cloning method by uracil excision[J]. Nucleic Acids Res, 2007, 35：1992-2002.
[36] Geu-Flores F, Nour-Eldin HH, Nielsen MT, et al. USER fusion：a rapid and efficient method for simultaneous fusion and cloning of multiple PCR products[J]. Nucleic Acids Res, 2007, 35：e55.
[37] Hutchins JR, Toyoda Y, Hegemann B, et al. Systematic analysis of human protein complexes identifies chromosome segregation proteins[J]. Science, 2010, 328：593-599.
[38] Musacchio A, Salmon ED. The spindle-assembly checkpoint in space and time[J]. Nat Rev Mol Cell Biol, 2007, 8：379-393.
[39] Chao WC, Kulkarni K, Zhang Z, et al. Structure of the mitotic checkpoint complex[J]. Nature, 2012, 484：208-213.
[40] Herzog F, Primorac I, Dube P, et al. Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex[J]. Science, 2009, 323：1477-1481.
[41] Cler E, Papai G, Schultz P, et al. Recent advances in understanding the structure and function of general transcription factor TFIID[J]. Cell Mol Life Sci, 2009, 66：2123-34.
[42] Muller F, Zaucker A, Tora L. Developmental regulation of transcrip-tion initiation：more than just changing the actors[J]. Curr Opin Genet Dev, 2010, 20：533-40.
[43] Papai G, Weil PA, Schultz P. New insights into the function of transcription factor TFIID from recent structural studies[J]. Curr Opin Genet Dev, 2011, 21：219-224.
[44] Wright KJ, Marr MT 2nd, Tjian R. TAF4 nucleates a core subcomplex of TFIID and mediates activated transcription from a TATA-less promoter[J]. Proc Natl Acad Sci USA, 2006, 103：12347-12352.
[45] Papai G, Tripathi MK, Ruhlmann C, et al. Mapping the initiator binding Taf2 subunit in the structure of hydrated yeast TFIID[J]. Structure, 2009, 17：363-373.
[46] Cianfrocco MA, Kassavetis GA, Grob P, et al. Human TFIID binds to core promoter DNA in a reorganized structural state[J]. Cell, 2013, 152：120-131.
[47] Sharon M, Robinson CV. The role of mass spectrometry in structure elucidation of dynamic protein complexes[J]. Annu Rev Biochem, 2007, 76：167-193.
[48] Bieniossek C, Papai G, Schaffitzel C, et al. The architecture of human general transcription factor TFIID core complex[J]. Nature, 2013, 493：699-702.
[49] Vijayachandran LS, Viola C, Garzoni F, et al. Robots, pipelines, polyproteins：enabling multiprotein expression in prokaryotic and eukaryotic cells[J]. J Struct Biol, 2011, 175：198-208.