메뉴 건너뛰기




Volumn 78, Issue 19, 2012, Pages 6838-6849

Identification and partial characterization of extracellular aspartic protease genes from Metschnikowia pulcherrima IWBT Y1123 and candida apicola IWBT Y1384

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEASE; AVAILABLE NITROGEN; BOVINE SERUM ALBUMINS; EXTRACELLULAR; EXTRACELLULAR ACIDS; GENE SEQUENCES; GRAPE JUICE; HAZE FORMATION; HETEROLOGOUS EXPRESSION; IN-SILICO; NON-SACCHAROMYCES; PARTIAL CHARACTERIZATION; PLATE ASSAY; PROTEASE ACTIVITIES; PUTATIVE PROTEINS; STRAIN-DEPENDENT; WINE YEAST;

EID: 84868307814     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00505-12     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 33644861572 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions
    • Albrecht A, et al. 2006. Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions. J. Biol. Chem. 281:688-694.
    • (2006) J. Biol. Chem. , vol.281 , pp. 688-694
    • Albrecht, A.1
  • 2
    • 0026010553 scopus 로고
    • Induction of secretory acid proteinase in Candida albicans
    • Banerjee A, Ganesan K, Datta A. 1991. Induction of secretory acid proteinase in Candida albicans. J. Gen. Microbiol. 137:2455-2461.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2455-2461
    • Banerjee, A.1    Ganesan, K.2    Datta, A.3
  • 5
    • 33745918646 scopus 로고    scopus 로고
    • Acidic extracellular proteases from microrganisms of fairly acidic niche
    • Bossi A, Bonizzato L, Zapparoli G. 2006. Acidic extracellular proteases from microrganisms of fairly acidic niche. Protein. Pept. Lett. 13:737-741.
    • (2006) Protein. Pept. Lett. , vol.13 , pp. 737-741
    • Bossi, A.1    Bonizzato, L.2    Zapparoli, G.3
  • 6
    • 0024374498 scopus 로고
    • Transcriptional control of the Saccharomyces cerevisiae PGK gene by RAPI
    • Chambers A, et al. 1989. Transcriptional control of the Saccharomyces cerevisiae PGK gene by RAPI. Mol. Cell. Biol. 9:5516-5524.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5516-5524
    • Chambers, A.1
  • 7
    • 0031487747 scopus 로고    scopus 로고
    • Screening of non-Saccharomyces wine yeasts for the presence of extracellular hydrolytic enzymes
    • Charoenchai C, Fleet GH, Henschke PA, Todd BENT. 1997. Screening of non-Saccharomyces wine yeasts for the presence of extracellular hydrolytic enzymes. Aust. J. Grape Wine Res. 3:2-8.
    • (1997) Aust. J. Grape Wine Res. , vol.3 , pp. 2-8
    • Charoenchai, C.1    Fleet, G.H.2    Henschke, P.A.3    Todd, B.4
  • 8
    • 79952008640 scopus 로고    scopus 로고
    • Non-Saccharomyces wine yeasts have a promising role in biotechnological approaches to winemaking
    • Ciani M, Comitini F. 2011. Non-Saccharomyces wine yeasts have a promising role in biotechnological approaches to winemaking. Ann. Microbiol. 61:25-32.
    • (2011) Ann. Microbiol. , vol.61 , pp. 25-32
    • Ciani, M.1    Comitini, F.2
  • 9
    • 0031945102 scopus 로고    scopus 로고
    • Oenological properties of non-Saccharomyces yeasts associated with wine-making
    • Ciani M, Maccarelli F. 1998. Oenological properties of non-Saccharomyces yeasts associated with wine-making. World J. Microbiol. Biotechnol. 14:199-203.
    • (1998) World J. Microbiol. Biotechnol. , vol.14 , pp. 199-203
    • Ciani, M.1    Maccarelli, F.2
  • 10
    • 84868333156 scopus 로고
    • Ausubel FM, et al (ed), Current protocols in molecular biology, vol 2.13.1. John Wiley, New York, NY
    • Collart MA, Oliviero S. 1993. Preparation of yeast RNA, p 13.12.1-13.12.5. In Ausubel FM, et al (ed), Current protocols in molecular biology, vol 2.13.1. John Wiley, New York, NY.
    • (1993) Preparation of yeast RNA
    • Collart, M.A.1    Oliviero, S.2
  • 11
    • 46949084992 scopus 로고    scopus 로고
    • A transcription factor regulatory cascade controls secreted aspartic protease expression in Candida albicans
    • Dabas N, Morschhäuser J. 2008. A transcription factor regulatory cascade controls secreted aspartic protease expression in Candida albicans. Mol. Microbiol. 69:586-602.
    • (2008) Mol. Microbiol. , vol.69 , pp. 586-602
    • Dabas, N.1    Morschhäuser, J.2
  • 12
    • 0025290527 scopus 로고
    • The structure and function of aspartic proteases
    • Davies DR. 1990. The structure and function of aspartic proteases. Annu. Rev. Biophys. Biophys. Chern. 19:189-215.
    • (1990) Annu. Rev. Biophys. Biophys. Chern. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 13
    • 3042720475 scopus 로고    scopus 로고
    • Genome evolution in yeasts
    • Dujon B, et al. 2004. Genome evolution in yeasts. Nature 430:35-44.
    • (2004) Nature , vol.430 , pp. 35-44
    • Dujon, B.1
  • 14
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn BM. 2002. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 102:4431-4458.
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 15
    • 0041870476 scopus 로고    scopus 로고
    • Yeast interactions and wine flavour
    • Fleet GH. 2003. Yeast interactions and wine flavour. Int. J. Food Microbiol. 86:11-22.
    • (2003) Int. J. Food Microbiol. , vol.86 , pp. 11-22
    • Fleet, G.H.1
  • 16
    • 50649117757 scopus 로고    scopus 로고
    • Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity
    • Folio P, Ritt J, Alexandre H, Remize F. 2008. Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity. Int. J. Food Microbiol. 127:26-31.
    • (2008) Int. J. Food Microbiol. , vol.127 , pp. 26-31
    • Folio, P.1    Ritt, J.2    Alexandre, H.3    Remize, F.4
  • 17
    • 0029263398 scopus 로고
    • Purification and properties of extracellular carboxyl proteinase secreted by Candida pulcherrima
    • Gotoh T, et al. 1995. Purification and properties of extracellular carboxyl proteinase secreted by Candida pulcherrima. Biosci. Biotechnol. Biochem. 59:367-371.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 367-371
    • Gotoh, T.1
  • 18
    • 33745863119 scopus 로고    scopus 로고
    • Development of a screening method for the identification of a novel Saccharomyces cerevisiae mutant over-expressing Trichoderma reesei cellobiohydrolase II
    • Gundllapalli S, Cordero Otero R, Pretorius IS. 2006. Development of a screening method for the identification of a novel Saccharomyces cerevisiae mutant over-expressing Trichoderma reesei cellobiohydrolase II. Ann. Microbiol. 56:143-150.
    • (2006) Ann. Microbiol. , vol.56 , pp. 143-150
    • Gundllapalli, S.1    Cordero Otero, R.2    Pretorius, I.S.3
  • 19
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman CS, Winston F. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57:267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 20
    • 0242641133 scopus 로고    scopus 로고
    • The use of Candida pulcherrima in combination with Saccharomyces cerevisiae for the production of Chenin blanc wine
    • Jolly NP, Augustyn OPH, Pretorius IS. 2003. The use of Candida pulcherrima in combination with Saccharomyces cerevisiae for the production of Chenin blanc wine. S. Afr. J. Enol. Vitic. 24:63-69.
    • (2003) S. Afr. J. Enol. Vitic. , vol.24 , pp. 63-69
    • Jolly, N.P.1    Augustyn, O.P.H.2    Pretorius, I.S.3
  • 22
    • 12244310145 scopus 로고    scopus 로고
    • The complete mitochondrial genome sequence of the pathogenic yeast Candida (Torulopsis) glabrata
    • Koszul R, et al. 2003. The complete mitochondrial genome sequence of the pathogenic yeast Candida (Torulopsis) glabrata. FEBS Lett. 534:39-48.
    • (2003) FEBS Lett , vol.534 , pp. 39-48
    • Koszul, R.1
  • 23
    • 0031792246 scopus 로고    scopus 로고
    • Identification and phylogeny of ascomycetous yeasts from analysis of nuclear large subunit (26S) ribosomal DNA partial sequences
    • Kurtzman CP, Robnett CJ. 1998. Identification and phylogeny of ascomycetous yeasts from analysis of nuclear large subunit (26S) ribosomal DNA partial sequences. Antonie Van Leeuwenhoek 73:331-371.
    • (1998) Antonie Van Leeuwenhoek , vol.73 , pp. 331-371
    • Kurtzman, C.P.1    Robnett, C.J.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277:680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0000632743 scopus 로고
    • Survey of yeast acid proteases for effectiveness of wine haze reduction
    • Lagace LS, Bisson LF. 1990. Survey of yeast acid proteases for effectiveness of wine haze reduction. Am. J. Enol. Vitic. 41:147-155.
    • (1990) Am. J. Enol. Vitic. , vol.41 , pp. 147-155
    • Lagace, L.S.1    Bisson, L.F.2
  • 27
    • 80052582862 scopus 로고    scopus 로고
    • Quantification of chitinase and thaumatin-like proteins in grape juices and wines
    • Le Bourse D, et al. 2011. Quantification of chitinase and thaumatin-like proteins in grape juices and wines. Anal. Bioanal. Chem. 401:1541-1549.
    • (2011) Anal. Bioanal. Chem. , vol.401 , pp. 1541-1549
    • Le Bourse, D.1
  • 28
    • 70350570671 scopus 로고    scopus 로고
    • Cloning and characterization of a novel aspartic protease gene from marine-derived Metschnikowia reukaufii and its expression in E. coli
    • Li J, et al. 2009. Cloning and characterization of a novel aspartic protease gene from marine-derived Metschnikowia reukaufii and its expression in E. coli. Appl. Biochem. Biotechnol. 159:119-132.
    • (2009) Appl. Biochem. Biotechnol. , vol.159 , pp. 119-132
    • Li, J.1
  • 29
    • 0031930895 scopus 로고    scopus 로고
    • Sequence analysis of the internal transcribed spacer 2 (ITS2) from yeast species within the genus Candida
    • Lott TJ, et al. 1998. Sequence analysis of the internal transcribed spacer 2 (ITS2) from yeast species within the genus Candida. Curr. Microbiol. 36:63-69.
    • (1998) Curr. Microbiol. , vol.36 , pp. 63-69
    • Lott, T.J.1
  • 30
    • 66149138708 scopus 로고    scopus 로고
    • Grape and wine proteins: their fractionation by hydrophobic interaction chromatography and identification by chromatographic and proteomic analysis
    • Marangon M, Van Sluyter SC, Haynes PA, Waters EJ. 2009. Grape and wine proteins: their fractionation by hydrophobic interaction chromatography and identification by chromatographic and proteomic analysis. J. Agric. Food Chem. 57:4415-4425.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 4415-4425
    • Marangon, M.1    Van Sluyter, S.C.2    Haynes, P.A.3    Waters, E.J.4
  • 31
    • 0030794656 scopus 로고    scopus 로고
    • Genetic regulation of nitrogen metabolism in the fungi
    • Marzluf GA. 1997. Genetic regulation of nitrogen metabolism in the fungi. Microbiol. Mol. Biol. Rev. 61:17-32.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 17-32
    • Marzluf, G.A.1
  • 32
    • 0032530681 scopus 로고    scopus 로고
    • Secretion and pH-dependent selfprocessing of the pro-form of the Yarrowia lipolytica acid extracellular protease
    • McEwen RK, Young TW. 1998. Secretion and pH-dependent selfprocessing of the pro-form of the Yarrowia lipolytica acid extracellular protease. Yeast 14:1115-1125.
    • (1998) Yeast , vol.14 , pp. 1115-1125
    • McEwen, R.K.1    Young, T.W.2
  • 33
    • 0023651185 scopus 로고
    • A transcriptional activator is located in the coding region of the yeast PGK gene
    • Mellor J, Dobson MJ, Kingsman AJ, Kingsman SM. 1987. A transcriptional activator is located in the coding region of the yeast PGK gene. Nucleic Acids Res. 15:6243-6259.
    • (1987) Nucleic Acids Res , vol.15 , pp. 6243-6259
    • Mellor, J.1    Dobson, M.J.2    Kingsman, A.J.3    Kingsman, S.M.4
  • 36
    • 79956355763 scopus 로고    scopus 로고
    • Nitrogen regulation of morphogenesis and protease secretion in Candida albicans
    • Morschhäuser J. 2011. Nitrogen regulation of morphogenesis and protease secretion in Candida albicans. Int. J. Med. Microbiol. 301:390-394.
    • (2011) Int. J. Med. Microbiol. , vol.301 , pp. 390-394
    • Morschhäuser, J.1
  • 37
    • 4544365934 scopus 로고    scopus 로고
    • Candida albicans proteinases and host/pathogen interactions
    • Naglik J, Albrecht A, Bader O, Hube B. 2004. Candida albicans proteinases and host/pathogen interactions. Cell. Microbiol. 6:915-926.
    • (2004) Cell. Microbiol. , vol.6 , pp. 915-926
    • Naglik, J.1    Albrecht, A.2    Bader, O.3    Hube, B.4
  • 38
    • 0030710147 scopus 로고    scopus 로고
    • KEX2 influences Candida albicans proteinase secretion and hyphal formation
    • Newport G, Agabian N. 1997. KEX2 influences Candida albicans proteinase secretion and hyphal formation. J. Biol. Chem. 272:28954-28961.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28954-28961
    • Newport, G.1    Agabian, N.2
  • 39
  • 40
    • 84987312044 scopus 로고
    • The release of yeast proteolytic enzymes into beer
    • Ormrod IHL, Lalor EF, Sharpe FR. 1991. The release of yeast proteolytic enzymes into beer. J. Inst. Brew. 97:441-443.
    • (1991) J. Inst. Brew. , vol.97 , pp. 441-443
    • Ormrod, I.H.L.1    Lalor, E.F.2    Sharpe, F.R.3
  • 41
    • 0037262145 scopus 로고    scopus 로고
    • Combined heat and proteolytic enzyme treatment of white wines reduces haze forming protein content without detrimental effect
    • Pocock KF, Høj PB, Adams KS, Kwiatkowski MJ, Waters EJ. 2003. Combined heat and proteolytic enzyme treatment of white wines reduces haze forming protein content without detrimental effect. Aust. J. Grape Wine Res. 9:56-63.
    • (2003) Aust. J. Grape Wine Res. , vol.9 , pp. 56-63
    • Pocock, K.F.1    Høj, P.B.2    Adams, K.S.3    Kwiatkowski, M.J.4    Waters, E.J.5
  • 44
    • 0034930779 scopus 로고    scopus 로고
    • Screening for the production of extracellular hydrolytic enzymes by non-Saccharomyces wine yeasts
    • Strauss MLA, Jolly NPNP, Lambrechts MG, Van Rensburg P. 2001. Screening for the production of extracellular hydrolytic enzymes by non-Saccharomyces wine yeasts. J. Appl. Microbiol. 91:182-190.
    • (2001) J. Appl. Microbiol. , vol.91 , pp. 182-190
    • Strauss, M.L.A.1    Jolly, N.P.N.P.2    Lambrechts, M.G.3    Van Rensburg, P.4
  • 45
    • 0029920879 scopus 로고    scopus 로고
    • Acid proteinase secreted by Candida tropicalis: functional analysis of preproregion cleavages in C. tropicalis and Saccharomyces cerevisiae
    • Togni G, Sanglard D, Quadroni M, Foundling SI, Monod M. 1996. Acid proteinase secreted by Candida tropicalis: functional analysis of preproregion cleavages in C. tropicalis and Saccharomyces cerevisiae. Microbiology 142:493-503.
    • (1996) Microbiology , vol.142 , pp. 493-503
    • Togni, G.1    Sanglard, D.2    Quadroni, M.3    Foundling, S.I.4    Monod, M.5
  • 46
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize β-strands in their active sites
    • Tyndall JDA, Nall T, Fairlie DP. 2005. Proteases universally recognize β-strands in their active sites. Chem. Rev. 105:973-1000.
    • (2005) Chem. Rev. , vol.105 , pp. 973-1000
    • Tyndall, J.D.A.1    Nall, T.2    Fairlie, D.P.3
  • 47
    • 13744253785 scopus 로고    scopus 로고
    • Mss11p is a central element of the regulatory network that controls FLO11 expression and invasive growth in Saccharomyces cerevisiae
    • Van Dyk D, Pretorius IS, Bauer FF. 2005. Mss11p is a central element of the regulatory network that controls FLO11 expression and invasive growth in Saccharomyces cerevisiae. Genetics 169:91-106.
    • (2005) Genetics , vol.169 , pp. 91-106
    • Van Dyk, D.1    Pretorius, I.S.2    Bauer, F.F.3
  • 48
    • 33744490033 scopus 로고    scopus 로고
    • Genetic engineering of an industrial strain of Saccharomyces cerevisiae for L-malic acid degradation via an efficient malo-ethanolic pathway
    • Volschenk H, et al. 2004. Genetic engineering of an industrial strain of Saccharomyces cerevisiae for L-malic acid degradation via an efficient malo-ethanolic pathway. S. Afr. J. Enol. Vitic. 25:63-73.
    • (2004) S. Afr. J. Enol. Vitic. , vol.25 , pp. 63-73
    • Volschenk, H.1
  • 49
    • 0001478358 scopus 로고
    • Identification of heat-unstable wine proteins and their resistance to peptidases
    • Waters EJ, Wallace W, Williams PJ. 1992. Identification of heat-unstable wine proteins and their resistance to peptidases. J. Agric. Food Chem. 40:1514-1519.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1514-1519
    • Waters, E.J.1    Wallace, W.2    Williams, P.J.3
  • 50
    • 0003125622 scopus 로고    scopus 로고
    • Nuisance proteins of wine are grape pathogenesis-related proteins
    • Waters EJ, Shirley NJ, Williams PJ. 1996. Nuisance proteins of wine are grape pathogenesis-related proteins. J. Agric. Food Chem. 44:3-5.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3-5
    • Waters, E.J.1    Shirley, N.J.2    Williams, P.J.3
  • 51
    • 23144439860 scopus 로고    scopus 로고
    • Preventing protein haze in bottled white wine
    • Waters EJ, et al. 2005. Preventing protein haze in bottled white wine. Aust. J. Grape Wine Res. 11:215-225.
    • (2005) Aust. J. Grape Wine Res. , vol.11 , pp. 215-225
    • Waters, E.J.1
  • 53
    • 0029853815 scopus 로고    scopus 로고
    • The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription
    • Young TW, et al. 1996. The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription. Microbiology 142: 2913-2921.
    • (1996) Microbiology , vol.142 , pp. 2913-2921
    • Young, T.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.