Enhanced cell-surface display and secretory production of cellulolytic enzymes with Saccharomyces cerevisiae Sed1 signal peptide

ABSTRACT Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzy...

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Published inBiotechnology and bioengineering Vol. 113; no. 11; pp. 2358 - 2366
Main Authors Inokuma, Kentaro, Bamba, Takahiro, Ishii, Jun, Ito, Yoichiro, Hasunuma, Tomohisa, Kondo, Akihiko
Format Journal Article
LanguageEnglish
Published United States Blackwell Publishing Ltd 01.11.2016
Wiley Subscription Services, Inc
Subjects
Anchoring
Aspergillus aculeatus
Baking yeast
Bioengineering
Biofuels
Cassettes
Cell Membrane - metabolism
Cell surface
cell surface display
Cell walls
Cellular biology
Cellulase - secretion
Cellulolytic enzymes
endo-glucanase
Endoglucanase
Enzymes
Ethanol
EXG1 protein
Fungi
Gene sequencing
Genes
Genetic Enhancement - methods
Genomes
Glucoamylase
Glucosidase
Glycosylphosphatidylinositol
Hypocrea jecorina
Lignocellulose
Localization
Mating
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Peptides
Pichia pastoris
Protein Engineering - methods
Protein Transport - genetics
Proteins
Recombinant
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Rhizopus oryzae
Saccharomyces cerevisiae
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Secretion
secretion signal sequence
Surface chemistry
Utilization
Yeast
Yeasts
β-glucosidase
Pichia pastoris
β-glucosidase
endo-glucanase
Saccharomyces cerevisiae
secretion signal sequence
cell surface display
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Abstract ABSTRACT Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell‐surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae α‐mating pheromone (MFα1SP) were constructed for cell‐surface display of Aspergillus aculeatus β‐glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell‐surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MFα1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3‐ and 1.9‐fold higher than the GLUASP and MFα1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell‐surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358–2366. © 2016 Wiley Periodicals, Inc. The effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene (SED1SP) for cell‐surface display and secretory production of heterologous enzymes is described. High secretion efficiency of the novel SP sequence was applicable for both cell‐surface display and secretory production of cellulolytic enzymes (BGL and EG) in S. cerevisiae. In addition, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris.
AbstractList Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell-surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae α-mating pheromone (MFα1SP) were constructed for cell-surface display of Aspergillus aculeatus β-glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell-surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MFα1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3- and 1.9-fold higher than the GLUASP and MFα1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell-surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358-2366. © 2016 Wiley Periodicals, Inc.
ABSTRACT Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell‐surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae α‐mating pheromone (MFα1SP) were constructed for cell‐surface display of Aspergillus aculeatus β‐glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell‐surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MFα1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3‐ and 1.9‐fold higher than the GLUASP and MFα1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell‐surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358–2366. © 2016 Wiley Periodicals, Inc. The effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene (SED1SP) for cell‐surface display and secretory production of heterologous enzymes is described. High secretion efficiency of the novel SP sequence was applicable for both cell‐surface display and secretory production of cellulolytic enzymes (BGL and EG) in S. cerevisiae. In addition, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris.
Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell-surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae [alpha]-mating pheromone (MF[alpha]1SP) were constructed for cell-surface display of Aspergillus aculeatus [beta]-glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell-surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MF[alpha]1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3- and 1.9-fold higher than the GLUASP and MF[alpha]1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell-surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358-2366. © 2016 Wiley Periodicals, Inc.
Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell-surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae α-mating pheromone (MFα1SP) were constructed for cell-surface display of Aspergillus aculeatus β-glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell-surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MFα1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3- and 1.9-fold higher than the GLUASP and MFα1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell-surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358-2366. © 2016 Wiley Periodicals, Inc.Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell-surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae α-mating pheromone (MFα1SP) were constructed for cell-surface display of Aspergillus aculeatus β-glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell-surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MFα1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3- and 1.9-fold higher than the GLUASP and MFα1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell-surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358-2366. © 2016 Wiley Periodicals, Inc.
Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene for cell-surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from S. cerevisiae SED1 (SED1SP), Rhizopus oryzae glucoamylase (GLUASP), and S. cerevisiae alpha -mating pheromone (MF alpha 1SP) were constructed for cell-surface display of Aspergillus aculeatus beta -glucosidase (BGL1) and Trichoderma reesei endoglucanase II (EGII). These gene cassettes were integrated into the S. cerevisiae genome. The recombinant strains with the SED1SP showed higher cell-surface BGL and EG activities than those with the conventional SP sequences (GLUASP and MF alpha 1SP). The novel SP sequence also improved the secretory production of BGL and EG in S. cerevisiae. The extracellular BGL activity of the recombinant strains with the SED1SP was 1.3- and 1.9-fold higher than the GLUASP and MF alpha 1SP strains, respectively. Moreover, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris. The utilization of the novel SP sequence is a promising option for highly efficient cell-surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016; 113: 2358-2366. The effectiveness of a novel signal peptide (SP) sequence derived from the Saccharomyces cerevisiae SED1 gene (SED1SP) for cell-surface display and secretory production of heterologous enzymes is described. High secretion efficiency of the novel SP sequence was applicable for both cell-surface display and secretory production of cellulolytic enzymes (BGL and EG) in S. cerevisiae. In addition, the utilization of SED1SP successfully enhanced the secretory production of BGL in Pichia pastoris.
Author Ishii, Jun
Ito, Yoichiro
Kondo, Akihiko
Bamba, Takahiro
Hasunuma, Tomohisa
Inokuma, Kentaro
Author_xml – sequence: 1
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  surname: Inokuma
  fullname: Inokuma, Kentaro
  organization: Organization of Advanced Science and Technology, Kobe University, Kobe, Japan
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  givenname: Takahiro
  surname: Bamba
  fullname: Bamba, Takahiro
  organization: Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan
– sequence: 3
  givenname: Jun
  surname: Ishii
  fullname: Ishii, Jun
  organization: Organization of Advanced Science and Technology, Kobe University, Kobe, Japan
– sequence: 4
  givenname: Yoichiro
  surname: Ito
  fullname: Ito, Yoichiro
  organization: Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan
– sequence: 5
  givenname: Tomohisa
  surname: Hasunuma
  fullname: Hasunuma, Tomohisa
  organization: Organization of Advanced Science and Technology, Kobe University, Kobe, Japan
– sequence: 6
  givenname: Akihiko
  surname: Kondo
  fullname: Kondo, Akihiko
  email: akondo@kobe-u.ac.jp
  organization: Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/27183011$$D View this record in MEDLINE/PubMed
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Issue 11
Keywords Pichia pastoris
β-glucosidase
endo-glucanase
Saccharomyces cerevisiae
secretion signal sequence
cell surface display
Language English
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PublicationTitle Biotechnology and bioengineering
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References Van Rooyen R, Hahn-Hägerdal B, La Grange DC, Van Zyl WH. 2005. Construction of cellobiose-growing and fermenting Saccharomyces cerevisiae strains. J Biotechnol 120(3):284-295.
Li J, Qian B, Yin J, Wu S, Zhuan F, Xu S, Li J, Salazar JK, Zhang W, Wang H. 2013. Surface display of recombinant Drosophila melanogaster acetylcholinesterase for detection of organic phosphorus and carbamate pesticides. PLoS ONE 8(9):e72986.
Kjærulff S, Jensen MR. 2005. Comparison of different signal peptides for secretion of heterologous proteins in fission yeast. Biochem Biophys Res Commun 336(3):974-982.
Wen F, Sun J, Zhao H. 2010. Yeast surface display of trifunctional minicellulosomes for simultaneous saccharification and fermentation of cellulose to ethanol. Appl Environ Microbiol 76(4):1251-1260.
Kida Y, Morimoto F, Sakaguchi M. 2009. Signal anchor sequence provides motive force for polypeptide chain translocation through the endoplasmic reticulum membrane. J Biol Chem 284(5):2861-2866.
Ng DT, Brown JD, Walter P. 1996. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 134(2):269-278.
Orlean P. 2012. Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall. Genetics 192(3):775-818.
Chen J, Zhou J, Sanders CK, Nolan JP, Cai H. 2009. A surface display yeast two-hybrid screening system for high-throughput protein interactome mapping. Anal Biochem 390(1):29-37.
Plath K, Mothes W, Wilkinson BM, Stirling CJ, Rapoport TA. 1998. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94(6):795-807.
Liu Z, Inokuma K, Ho SH, Haan R, Hasunuma T, Van Zyl WH, Kondo A. 2015. Combined cell-surface display- and secretion-based strategies for production of cellulosic ethanol with Saccharomyces cerevisiae. Biotechnol Biofuels 8:162.
Kim S, Baek SH, Lee K, Hahn JS. 2013. Cellulosic ethanol production using a yeast consortium displaying a minicellulosome and β-glucosidase. Microb Cell Fact 12:14.
Lee MA, Cheong KH, Shields D, Park SD, Hong SH. 2002. Intracellular trafficking and metabolic turnover of yeast prepro-α-factor-SRIF precursors in GH3 cells. Exp Mol Med 34(4):285-293.
Kurjan J, Herskowitz I. 1982. Structure of a yeast pheromone gene (MFα): A putative α-factor precursor contains four tandem copies of mature α-factor. Cell 30(3):933-943
Horton P, Park KJ, Obayashi T, Fujita N, Harada H, Adams-Collier CJ, Nakai K. 2007. WoLF PSORT: Protein localization predictor. Nucleic Acids Res 35(Web Server issue):W585-W587.
Näätsaari L, Mistlberger B, Ruth C, Hajek T, Hartner FS, Glieder A. 2012. Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology. PLoS ONE 7(6):e39720.
Fan LH, Zhang ZJ, Yu XY, Xue YX, Tan TW. 2012. Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellulosic ethanol production. Proc Natl Acad Sci USA 109(33):13260-13265.
Rakestraw JA, Sazinsky SL, Piatesi A, Antipov E, Wittrup KD. 2009. Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies in Saccharomyces cerevisiae. Biotechnol Bioeng 103(6):1192-1201.
Gibson DG, Young L, Chuang RY, Venter JC, Hutchison CA, 3rd, Smith HO. 2009. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods 6(5):343-345.
Gasser B, Prielhofer R, Marx H, Maurer M, Nocon J, Steiger M, Puxbaum V, Sauer M, Mattanovich D. 2013. Pichia pastoris: Protein production host and model organism for biomedical research. Future Microbiol 8(2):191-208.
Ismail KS, Sakamoto T, Hatanaka H, Hasunuma T, Kondo A. 2013. Gene expression cross-profiling in genetically modified industrial Saccharomyces cerevisiae strains during high-temperature ethanol production from xylose. J Biotechnol 163(1):50-60.
Guo ZP, Qiu CY, Zhang L, Ding ZY, Wang ZX, Shi GY. 2011. Expression of aspartic protease from Neurospora crassa in industrial ethanol-producing yeast and its application in ethanol production. Enzyme Microb Technol 48(2):148-154.
Yarimizu T, Nakamura M, Hoshida H, Akada R. 2015. Synthetic signal sequences that enable efficient secretory protein production in the yeast Kluyveromyces marxianus. Microb Cell Fact 14:20.
Fujita Y, Ito J, Ueda M, Fukuda H, Kondo A. 2004. Synergistic saccharification, and direct fermentation to ethanol, of amorphous cellulose by use of an engineered yeast strain codisplaying three types of cellulolytic enzyme. Appl Environ Microbiol 70(2):1207-1212.
Yamakawa S, Yamada R, Tanaka T, Ogino C, Kondo A. 2012. Repeated fermentation from raw starch using Saccharomyces cerevisiae displaying both glucoamylase and α-amylase. Enzyme Microb Technol 50(6-7):343-347.
Chen DC, Yang BC, Kuo TT. 1992. One-step transformation of yeast in stationary phase. Curr Genet 21(1):83-84.
Yanase S, Hasunuma T, Yamada R, Tanaka T, Ogino C, Fukuda H, Kondo A. 2010. Direct ethanol production from cellulosic materials at high temperature using the thermotolerant yeast Kluyveromyces marxianus displaying cellulolytic enzymes. Appl Microbiol Biotechnol 88(1):381-388.
Ueda M, Tanaka A. 2000. Cell surface engineering of yeast: Construction of arming yeast with biocatalyst. J Biosci Bioeng 90(2):125-136.
Kamiya T, Ojima T, Sugimoto K, Nakano H, Kawarasaki Y. 2010. Quantitative Y2H screening: Cloning and signal peptide engineering of a fungal secretory LacA gene and its application to yeast two-hybrid system as a quantitative reporter. J Biotechnol 146(4):151-159.
Yamada R, Taniguchi N, Tanaka T, Ogino C, Fukuda H, Kondo A. 2011. Direct ethanol production from cellulosic materials using a diploid strain of Saccharomyces cerevisiae with optimized cellulase expression. Biotechnol Biofuels 4:8.
Kondo A, Ueda M. 2004. Yeast cell-surface display-applications of molecular display. Appl Microbiol Biotechnol 64(1):28-40.
Inokuma K, Hasunuma T, Kondo A. 2014. Efficient yeast cell-surface display of exo- and endo-cellulase using the SED1 anchoring region and its original promoter. Biotechnol Biofuels 7(1):8.
Ahmad M, Hirz M, Pichler H, Schwab H. 2014. Protein expression in Pichia pastoris: Recent achievements and perspectives for heterologous protein production. Appl Microbiol Biotechnol 98(12):5301-5317.
Kotaka A, Bando H, Kaya M, Kato-Murai M, Kuroda K, Sahara H, Hata Y, Kondo A, Ueda M. 2008. Direct ethanol production from barley β-glucan by sake yeast displaying Aspergillus oryzae β-glucosidase and endoglucanase. J Biosci Bioeng 105(6):622-627.
Goyal G, Tsai SL, Madan B, DaSilva NA, Chen W. 2011. Simultaneous cell growth and ethanol production from cellulose by an engineered yeast consortium displaying a functional mini-cellulosome. Microb Cell Fact 10:89.
Oka C, Tanaka M, Muraki M, Harata K, Suzuki K, Jigami Y. 1999. Human lysozyme secretion increased by alpha-factor pro-sequence in Pichia pastoris. Biosci Biotechnol Biochem 63(11):1977-1983.
Shimoi H, Kitagaki H, Ohmori H, Iimura Y, Ito K. 1998. Sed1p is a major cell wall protein of Saccharomyces cerevisiae in the stationary phase and is involved in lytic enzyme resistance. J Bacteriol 180(13):3381-3387.
Yamada R, Taniguchi N, Tanaka T, Ogino C, Fukuda H, Kondo A. 2010. Cocktail δ-integration: A novel method to construct cellulolytic enzyme expression ratio-optimized yeast strains. Microb Cell Fact 9:32.
Martoglio B, Dobberstein B. 1998. Signal sequences: More than just greasy peptides. Trends Cell Biol 8(10):410-415.
Inokuma K, Yoshida T, Ishii J, Hasunuma T, Kondo A. 2015. Efficient co-displaying and artificial ratio control of α-amylase and glucoamylase on the yeast cell surface by using combinations of different anchoring domains. Appl Microbiol Biotechnol 99(4):1655-1663.
Dashtban M, Schraft H, Qin W. 2009. Fungal bioconversion of lignocellulosic residues; opportunities & perspectives. Int J Biol Sci 5(6):578-595.
Mori A, Hara S, Sugahara T, Kojima T, Iwasaki Y, Kawarasaki Y, Sahara T, Ohgiya S, Nakano H. 2015. Signal peptide optimization tool for the secretion of recombinant protein from Saccharomyces cerevisiae. J Biosci Bioeng 120(5):518-525.
Idiris A, Tohda H, Kumagai H, Takegawa K. 2010. Engineering of protein secretion in yeast: Strategies and impact on protein production. Appl Microbiol Biotechnol 86(2):403-417.
Ishii J, Izawa K, Matsumura S, Wakamura K, Tanino T, Tanaka T, Ogino C, Fukuda H, Kondo A. 2009. A simple and immediate method for simultaneously evaluating expression level and plasmid maintenance in yeast. J Biochem 145(6):701-708.
1998; 180
2010; 76
2004; 64
2015; 14
1982; 30
2002; 34
2015; 99
2005; 336
2015; 120
2010; 146
2011; 10
2013; 163
2008; 105
2000; 90
1999; 63
2011; 4
2013; 8
2015; 8
2007; 35
2012; 109
2012; 50
2010; 88
2010; 86
2004; 70
2005; 120
2009; 390
2013; 12
2012; 192
2009; 145
2009; 6
2009; 5
2011; 48
2009; 284
1998; 94
1992; 21
2012; 7
2014; 7
1996; 134
2009; 103
2014; 98
2010; 9
1998; 8
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References_xml – reference: Kotaka A, Bando H, Kaya M, Kato-Murai M, Kuroda K, Sahara H, Hata Y, Kondo A, Ueda M. 2008. Direct ethanol production from barley β-glucan by sake yeast displaying Aspergillus oryzae β-glucosidase and endoglucanase. J Biosci Bioeng 105(6):622-627.
– reference: Guo ZP, Qiu CY, Zhang L, Ding ZY, Wang ZX, Shi GY. 2011. Expression of aspartic protease from Neurospora crassa in industrial ethanol-producing yeast and its application in ethanol production. Enzyme Microb Technol 48(2):148-154.
– reference: Lee MA, Cheong KH, Shields D, Park SD, Hong SH. 2002. Intracellular trafficking and metabolic turnover of yeast prepro-α-factor-SRIF precursors in GH3 cells. Exp Mol Med 34(4):285-293.
– reference: Yanase S, Hasunuma T, Yamada R, Tanaka T, Ogino C, Fukuda H, Kondo A. 2010. Direct ethanol production from cellulosic materials at high temperature using the thermotolerant yeast Kluyveromyces marxianus displaying cellulolytic enzymes. Appl Microbiol Biotechnol 88(1):381-388.
– reference: Wen F, Sun J, Zhao H. 2010. Yeast surface display of trifunctional minicellulosomes for simultaneous saccharification and fermentation of cellulose to ethanol. Appl Environ Microbiol 76(4):1251-1260.
– reference: Chen DC, Yang BC, Kuo TT. 1992. One-step transformation of yeast in stationary phase. Curr Genet 21(1):83-84.
– reference: Orlean P. 2012. Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall. Genetics 192(3):775-818.
– reference: Ahmad M, Hirz M, Pichler H, Schwab H. 2014. Protein expression in Pichia pastoris: Recent achievements and perspectives for heterologous protein production. Appl Microbiol Biotechnol 98(12):5301-5317.
– reference: Martoglio B, Dobberstein B. 1998. Signal sequences: More than just greasy peptides. Trends Cell Biol 8(10):410-415.
– reference: Fujita Y, Ito J, Ueda M, Fukuda H, Kondo A. 2004. Synergistic saccharification, and direct fermentation to ethanol, of amorphous cellulose by use of an engineered yeast strain codisplaying three types of cellulolytic enzyme. Appl Environ Microbiol 70(2):1207-1212.
– reference: Gibson DG, Young L, Chuang RY, Venter JC, Hutchison CA, 3rd, Smith HO. 2009. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods 6(5):343-345.
– reference: Idiris A, Tohda H, Kumagai H, Takegawa K. 2010. Engineering of protein secretion in yeast: Strategies and impact on protein production. Appl Microbiol Biotechnol 86(2):403-417.
– reference: Oka C, Tanaka M, Muraki M, Harata K, Suzuki K, Jigami Y. 1999. Human lysozyme secretion increased by alpha-factor pro-sequence in Pichia pastoris. Biosci Biotechnol Biochem 63(11):1977-1983.
– reference: Rakestraw JA, Sazinsky SL, Piatesi A, Antipov E, Wittrup KD. 2009. Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies in Saccharomyces cerevisiae. Biotechnol Bioeng 103(6):1192-1201.
– reference: Mori A, Hara S, Sugahara T, Kojima T, Iwasaki Y, Kawarasaki Y, Sahara T, Ohgiya S, Nakano H. 2015. Signal peptide optimization tool for the secretion of recombinant protein from Saccharomyces cerevisiae. J Biosci Bioeng 120(5):518-525.
– reference: Fan LH, Zhang ZJ, Yu XY, Xue YX, Tan TW. 2012. Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellulosic ethanol production. Proc Natl Acad Sci USA 109(33):13260-13265.
– reference: Horton P, Park KJ, Obayashi T, Fujita N, Harada H, Adams-Collier CJ, Nakai K. 2007. WoLF PSORT: Protein localization predictor. Nucleic Acids Res 35(Web Server issue):W585-W587.
– reference: Kurjan J, Herskowitz I. 1982. Structure of a yeast pheromone gene (MFα): A putative α-factor precursor contains four tandem copies of mature α-factor. Cell 30(3):933-943
– reference: Kamiya T, Ojima T, Sugimoto K, Nakano H, Kawarasaki Y. 2010. Quantitative Y2H screening: Cloning and signal peptide engineering of a fungal secretory LacA gene and its application to yeast two-hybrid system as a quantitative reporter. J Biotechnol 146(4):151-159.
– reference: Kjærulff S, Jensen MR. 2005. Comparison of different signal peptides for secretion of heterologous proteins in fission yeast. Biochem Biophys Res Commun 336(3):974-982.
– reference: Dashtban M, Schraft H, Qin W. 2009. Fungal bioconversion of lignocellulosic residues; opportunities & perspectives. Int J Biol Sci 5(6):578-595.
– reference: Kim S, Baek SH, Lee K, Hahn JS. 2013. Cellulosic ethanol production using a yeast consortium displaying a minicellulosome and β-glucosidase. Microb Cell Fact 12:14.
– reference: Ishii J, Izawa K, Matsumura S, Wakamura K, Tanino T, Tanaka T, Ogino C, Fukuda H, Kondo A. 2009. A simple and immediate method for simultaneously evaluating expression level and plasmid maintenance in yeast. J Biochem 145(6):701-708.
– reference: Shimoi H, Kitagaki H, Ohmori H, Iimura Y, Ito K. 1998. Sed1p is a major cell wall protein of Saccharomyces cerevisiae in the stationary phase and is involved in lytic enzyme resistance. J Bacteriol 180(13):3381-3387.
– reference: Näätsaari L, Mistlberger B, Ruth C, Hajek T, Hartner FS, Glieder A. 2012. Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology. PLoS ONE 7(6):e39720.
– reference: Liu Z, Inokuma K, Ho SH, Haan R, Hasunuma T, Van Zyl WH, Kondo A. 2015. Combined cell-surface display- and secretion-based strategies for production of cellulosic ethanol with Saccharomyces cerevisiae. Biotechnol Biofuels 8:162.
– reference: Inokuma K, Yoshida T, Ishii J, Hasunuma T, Kondo A. 2015. Efficient co-displaying and artificial ratio control of α-amylase and glucoamylase on the yeast cell surface by using combinations of different anchoring domains. Appl Microbiol Biotechnol 99(4):1655-1663.
– reference: Inokuma K, Hasunuma T, Kondo A. 2014. Efficient yeast cell-surface display of exo- and endo-cellulase using the SED1 anchoring region and its original promoter. Biotechnol Biofuels 7(1):8.
– reference: Ismail KS, Sakamoto T, Hatanaka H, Hasunuma T, Kondo A. 2013. Gene expression cross-profiling in genetically modified industrial Saccharomyces cerevisiae strains during high-temperature ethanol production from xylose. J Biotechnol 163(1):50-60.
– reference: Yamada R, Taniguchi N, Tanaka T, Ogino C, Fukuda H, Kondo A. 2010. Cocktail δ-integration: A novel method to construct cellulolytic enzyme expression ratio-optimized yeast strains. Microb Cell Fact 9:32.
– reference: Li J, Qian B, Yin J, Wu S, Zhuan F, Xu S, Li J, Salazar JK, Zhang W, Wang H. 2013. Surface display of recombinant Drosophila melanogaster acetylcholinesterase for detection of organic phosphorus and carbamate pesticides. PLoS ONE 8(9):e72986.
– reference: Yamada R, Taniguchi N, Tanaka T, Ogino C, Fukuda H, Kondo A. 2011. Direct ethanol production from cellulosic materials using a diploid strain of Saccharomyces cerevisiae with optimized cellulase expression. Biotechnol Biofuels 4:8.
– reference: Gasser B, Prielhofer R, Marx H, Maurer M, Nocon J, Steiger M, Puxbaum V, Sauer M, Mattanovich D. 2013. Pichia pastoris: Protein production host and model organism for biomedical research. Future Microbiol 8(2):191-208.
– reference: Kondo A, Ueda M. 2004. Yeast cell-surface display-applications of molecular display. Appl Microbiol Biotechnol 64(1):28-40.
– reference: Plath K, Mothes W, Wilkinson BM, Stirling CJ, Rapoport TA. 1998. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94(6):795-807.
– reference: Ueda M, Tanaka A. 2000. Cell surface engineering of yeast: Construction of arming yeast with biocatalyst. J Biosci Bioeng 90(2):125-136.
– reference: Van Rooyen R, Hahn-Hägerdal B, La Grange DC, Van Zyl WH. 2005. Construction of cellobiose-growing and fermenting Saccharomyces cerevisiae strains. J Biotechnol 120(3):284-295.
– reference: Kida Y, Morimoto F, Sakaguchi M. 2009. Signal anchor sequence provides motive force for polypeptide chain translocation through the endoplasmic reticulum membrane. J Biol Chem 284(5):2861-2866.
– reference: Yarimizu T, Nakamura M, Hoshida H, Akada R. 2015. Synthetic signal sequences that enable efficient secretory protein production in the yeast Kluyveromyces marxianus. Microb Cell Fact 14:20.
– reference: Yamakawa S, Yamada R, Tanaka T, Ogino C, Kondo A. 2012. Repeated fermentation from raw starch using Saccharomyces cerevisiae displaying both glucoamylase and α-amylase. Enzyme Microb Technol 50(6-7):343-347.
– reference: Goyal G, Tsai SL, Madan B, DaSilva NA, Chen W. 2011. Simultaneous cell growth and ethanol production from cellulose by an engineered yeast consortium displaying a functional mini-cellulosome. Microb Cell Fact 10:89.
– reference: Chen J, Zhou J, Sanders CK, Nolan JP, Cai H. 2009. A surface display yeast two-hybrid screening system for high-throughput protein interactome mapping. Anal Biochem 390(1):29-37.
– reference: Ng DT, Brown JD, Walter P. 1996. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 134(2):269-278.
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  year: 2013
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– volume: 34
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  issue: 6
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– volume: 88
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  year: 2010
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  publication-title: Appl Microbiol Biotechnol
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  article-title: Signal sequences specify the targeting route to the endoplasmic reticulum membrane
  publication-title: J Cell Biol
– volume: 8
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  year: 2015
  article-title: Combined cell‐surface display‐ and secretion‐based strategies for production of cellulosic ethanol with
  publication-title: Biotechnol Biofuels
– volume: 8
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  issue: 10
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  end-page: 415
  article-title: Signal sequences: More than just greasy peptides
  publication-title: Trends Cell Biol
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Snippet ABSTRACT Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring...
Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are...
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SubjectTerms Anchoring
Aspergillus aculeatus
Baking yeast
Bioengineering
Biofuels
Cassettes
Cell Membrane - metabolism
Cell surface
cell surface display
Cell walls
Cellular biology
Cellulase - secretion
Cellulolytic enzymes
endo-glucanase
Endoglucanase
Enzymes
Ethanol
EXG1 protein
Fungi
Gene sequencing
Genes
Genetic Enhancement - methods
Genomes
Glucoamylase
Glucosidase
Glycosylphosphatidylinositol
Hypocrea jecorina
Lignocellulose
Localization
Mating
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Peptides
Pichia pastoris
Protein Engineering - methods
Protein Transport - genetics
Proteins
Recombinant
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Rhizopus oryzae
Saccharomyces cerevisiae
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Secretion
secretion signal sequence
Surface chemistry
Utilization
Yeast
Yeasts
β-glucosidase
Title Enhanced cell-surface display and secretory production of cellulolytic enzymes with Saccharomyces cerevisiae Sed1 signal peptide
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