메뉴 건너뛰기




Volumn 98, Issue 3, 2014, Pages 1185-1194

Characterization of genes for chitin catabolism in Haloferax mediterranei

Author keywords

Bioconversion; Bioplastic; Catabolism; Chitin; Haloarchaea

Indexed keywords

BIOCHEMISTRY; BIOCONVERSION; CELL GROWTH; CELL PROLIFERATION; ENZYMES; GROWTH KINETICS; METABOLISM; POLYMERASE CHAIN REACTION; SOLS; TRANSCRIPTION;

EID: 84898897999     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-4969-8     Document Type: Article
Times cited : (31)

References (33)
  • 1
    • 8644220387 scopus 로고    scopus 로고
    • Multiple components and induction mechanism of the chitinolytic system of the hyperthermophilic archaeon Thermococcus chitonophagus
    • 10.1007/s00253-004-1640-4 15322771 10.1007/s00253-004-1640-4
    • Andronopoulou E, Vorgias CE (2004) Multiple components and induction mechanism of the chitinolytic system of the hyperthermophilic archaeon Thermococcus chitonophagus. Appl Microbiol Biotechnol 65:694-702. doi: 10.1007/s00253-004-1640-4
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 694-702
    • Andronopoulou, E.1    Vorgias, C.E.2
  • 2
    • 84863229520 scopus 로고    scopus 로고
    • Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei
    • 10.1128/AEM.07114-11 3298179 22247127 10.1128/AEM.07114-11
    • Cai S, Cai L, Liu H, Liu X, Han J, Zhou J, Xiang H (2012) Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei. Appl Environ Microbiol 78:1946-1952. doi: 10.1128/AEM.07114-11
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1946-1952
    • Cai, S.1    Cai, L.2    Liu, H.3    Liu, X.4    Han, J.5    Zhou, J.6    Xiang, H.7
  • 3
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • 10.1016/S0958-1669(98)80058-X 9650272 10.1016/S0958-1669(98)80058-X
    • Cohen-Kupiec R, Chet I (1998) The molecular biology of chitin digestion. Curr Opin Biotechnol 9:270-277. doi: 10.1016/S0958-1669(98)80058-X
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 4
    • 0036204403 scopus 로고    scopus 로고
    • The family-3 glycoside hydrolases: From housekeeping functions to host-microbe interactions
    • 10.1128/AEM.68.4.1485-1490.2002 123870 11916659 10.1128/AEM.68.4.1485-1490.2002
    • Faure D (2002) The family-3 glycoside hydrolases: from housekeeping functions to host-microbe interactions. Appl Environ Microbiol 68:1485-1490. doi: 10.1128/AEM.68.4.1485-1490.2002
    • (2002) Appl Environ Microbiol , vol.68 , pp. 1485-1490
    • Faure, D.1
  • 5
    • 0038317570 scopus 로고    scopus 로고
    • Growth of hyperthermophilic archaeon Pyrococcus futiosus on chitin involves two family 18 chitinases
    • 10.1128/AEM.69.6.3119-3128.2003 161489 12788706 10.1128/AEM.69.6.3119-3128.2003
    • Gao J, Bauer MW, Shockley KR, Pysz MA, Kelly RM (2003) Growth of hyperthermophilic archaeon Pyrococcus futiosus on chitin involves two family 18 chitinases. Appl Environ Microbiol 69:3119-3128. doi: 10.1128/AEM.69.6.3119-3128.2003
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3119-3128
    • Gao, J.1    Bauer, M.W.2    Shockley, K.R.3    Pysz, M.A.4    Kelly, R.M.5
  • 6
    • 35148828068 scopus 로고    scopus 로고
    • Hm genes, required for biosynthesis of poly(3-hydroxybutyrate) in the extremely halophilic archaeon Haloarcula marismortui
    • 10.1128/AEM.00953-07 2075026 17675423 10.1128/AEM.00953-07
    • Hm genes, required for biosynthesis of poly(3-hydroxybutyrate) in the extremely halophilic archaeon Haloarcula marismortui. Appl Environ Microbiol 73:6058-6065. doi: 10.1128/AEM.00953-07
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6058-6065
    • Han, J.1    Lu, Q.2    Zhou, L.3    Zhou, J.4    Xiang, H.5
  • 7
    • 84866320274 scopus 로고    scopus 로고
    • Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer
    • 10.1128/JB.00880-12 3416209 22843593 10.1128/JB.00880-12
    • Han J, Zhang F, Hou J, Liu XQ, Li M, Liu HL, Cai L, Zhang B, Chen YP, Zhou J, Hu SN, Xiang H (2012) Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer. J Bacteriol 194:4463-4464. doi: 10.1128/JB.00880-12
    • (2012) J Bacteriol , vol.194 , pp. 4463-4464
    • Han, J.1    Zhang, F.2    Hou, J.3    Liu, X.Q.4    Li, M.5    Liu, H.L.6    Cai, L.7    Zhang, B.8    Chen, Y.P.9    Zhou, J.10    Hu, S.N.11    Xiang, H.12
  • 8
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance: Engineering plants and enzymes for biofuels production
    • 10.1126/science.1137016 17289988 10.1126/science.1137016
    • Himmel ME, Ding SY, Johnson DK, Adney WS, Nimlos MR, Brady JW, Foust TD (2007) Biomass recalcitrance: engineering plants and enzymes for biofuels production. Science 315:804-807. doi: 10.1126/science.1137016
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1    Ding, S.Y.2    Johnson, D.K.3    Adney, W.S.4    Nimlos, M.R.5    Brady, J.W.6    Foust, T.D.7
  • 9
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • 10.1271/bbb1961.35.1154
    • Imoto T, Yagishita K (1971) A simple activity measurement of lysozyme. Agric Biol Chem 35:1154-1156
    • (1971) Agric Biol Chem , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 10
    • 60149095281 scopus 로고    scopus 로고
    • Evolution of family 18 glycoside hydrolases: Diversity, domain structures and phylogenetic relationships
    • 10.1159/000151220 18679019 10.1159/000151220
    • Karlsson M, Stenlid J (2009) Evolution of family 18 glycoside hydrolases: diversity, domain structures and phylogenetic relationships. J Mol Microbiol Biotechnol 16:208-223. doi: 10.1159/000151220
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 208-223
    • Karlsson, M.1    Stenlid, J.2
  • 11
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic β-N-acetylglucosaminidase
    • 10.1074/jbc.271.52.33425 8969205 10.1074/jbc.271.52.33425
    • Keyhani NO, Roseman S (1996) The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic β-N-acetylglucosaminidase. J Biol Chem 271:33425-33432. doi: 10.1074/jbc.271.52.33425
    • (1996) J Biol Chem , vol.271 , pp. 33425-33432
    • Keyhani, N.O.1    Roseman, S.2
  • 12
    • 84873333675 scopus 로고    scopus 로고
    • Genetic engineering of Pyrococcus furiosus to use chitin as a carbon source
    • 10.1186/1472-6750-13-9 3575233 23391022 10.1186/1472-6750-13-9
    • Kreuzer M, Schmutzler K, Waege I, Thomm M, Hausner W (2013) Genetic engineering of Pyrococcus furiosus to use chitin as a carbon source. BMC Biotechnol 13:9. doi: 10.1186/1472-6750-13-9
    • (2013) BMC Biotechnol , vol.13 , pp. 9
    • Kreuzer, M.1    Schmutzler, K.2    Waege, I.3    Thomm, M.4    Hausner, W.5
  • 13
    • 33745091826 scopus 로고    scopus 로고
    • Chitin and chitosan: Functional biopolymers from marine crustaceans
    • 10.1007/s10126-005-0097-5 10.1007/s10126-005-0097-5
    • Kurita K (2006) Chitin and chitosan: functional biopolymers from marine crustaceans. Mar Biotechnol (NY) 8:203-226. doi: 10.1007/s10126-005-0097-5
    • (2006) Mar Biotechnol (NY) , vol.8 , pp. 203-226
    • Kurita, K.1
  • 14
    • 77952486301 scopus 로고    scopus 로고
    • Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding
    • 10.1371/journal.pone.0008654 2805709 20084296 10.1371/journal.pone.0008654
    • Li H, Greene LH (2010) Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding. PLoS One 5:e8654. doi: 10.1371/journal.pone.0008654
    • (2010) PLoS One , vol.5 , pp. 8654
    • Li, H.1    Greene, L.H.2
  • 15
    • 79959374305 scopus 로고    scopus 로고
    • Development of pyrF-based gene knockout systems for genome-wide manipulation of the archaea Haloferax mediterranei and Haloarcula hispanica
    • 10.1016/j.jgg.2011.05.003 21703550 10.1016/j.jgg.2011.05.003
    • Liu HL, Han J, Liu XQ, Zhou J, Xiang H (2011) Development of pyrF-based gene knockout systems for genome-wide manipulation of the archaea Haloferax mediterranei and Haloarcula hispanica. J Genet Genomics 38:261-269. doi: 10.1016/j.jgg.2011.05.003
    • (2011) J Genet Genomics , vol.38 , pp. 261-269
    • Liu, H.L.1    Han, J.2    Liu, X.Q.3    Zhou, J.4    Xiang, H.5
  • 16
    • 44349164550 scopus 로고    scopus 로고
    • Dissection of the regulatory mechanism of a heat-shock responsive promoter in Haloarchaea: A new paradigm for general transcription factor directed archaeal gene regulation
    • 10.1093/nar/gkn152 2396416 18390887 10.1093/nar/gkn152
    • Lu Q, Han J, Zhou L, Coker JA, DasSarma P, DasSarma S, Xiang H (2008a) Dissection of the regulatory mechanism of a heat-shock responsive promoter in Haloarchaea: a new paradigm for general transcription factor directed archaeal gene regulation. Nucleic Acids Res 36:3031-3042. doi: 10.1093/nar/gkn152
    • (2008) Nucleic Acids Res , vol.36 , pp. 3031-3042
    • Lu, Q.1    Han, J.2    Zhou, L.3    Coker, J.A.4    Dassarma, P.5    Dassarma, S.6    Xiang, H.7
  • 17
    • 44949083652 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthase in Haloferax mediterranei
    • 10.1128/JB.00134-08 2446746 18408025 10.1128/JB.00134-08
    • Lu QH, Han J, Zhou LG, Zhou J, Xiang H (2008b) Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthase in Haloferax mediterranei. J Bacteriol 190:4173-4180. doi: 10.1128/JB.00134-08
    • (2008) J Bacteriol , vol.190 , pp. 4173-4180
    • Lu, Q.H.1    Han, J.2    Zhou, L.G.3    Zhou, J.4    Xiang, H.5
  • 18
    • 68949127197 scopus 로고    scopus 로고
    • Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1
    • 10.1007/s10719-008-9203-z 18975073 10.1007/s10719-008-9203-z
    • Lü Y, Yang H, Hu H, Wang Y, Rao Z, Jin C (2009) Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1. Glycoconj J 26:525-534. doi: 10.1007/s10719-008-9203-z
    • (2009) Glycoconj J , vol.26 , pp. 525-534
    • Lü, Y.1    Yang, H.2    Hu, H.3    Wang, Y.4    Rao, Z.5    Jin, C.6
  • 20
    • 0001516452 scopus 로고
    • Chitin and chitosan, versatile polysaccharides from marine animals
    • 10.1021/ed067p938 10.1021/ed067p938
    • Mathur NK, Narang CK (1990) Chitin and chitosan, versatile polysaccharides from marine animals. J Chem Educ 67:938-942. doi: 10.1021/ed067p938
    • (1990) J Chem Educ , vol.67 , pp. 938-942
    • Mathur, N.K.1    Narang, C.K.2
  • 21
    • 47849085074 scopus 로고    scopus 로고
    • Tertiary structure and carbohydrate recognition by the chitin-binding domain of a hyperthermophilic chitinase from Pyrococcus furiosus
    • 10.1016/j.jmb.2008.06.006 18582475 10.1016/j.jmb.2008.06.006
    • Nakamura T, Mine S, Hagihara Y, Ishikawa K, Ikegami T, Uegaki K (2008) Tertiary structure and carbohydrate recognition by the chitin-binding domain of a hyperthermophilic chitinase from Pyrococcus furiosus. J Mol Biol 381:670-680. doi: 10.1016/j.jmb.2008.06.006
    • (2008) J Mol Biol , vol.381 , pp. 670-680
    • Nakamura, T.1    Mine, S.2    Hagihara, Y.3    Ishikawa, K.4    Ikegami, T.5    Uegaki, K.6
  • 22
    • 33746449573 scopus 로고    scopus 로고
    • Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: Activity toward crystalline chitin
    • 10.1271/bbb.60031 16861805 10.1271/bbb.60031
    • Oku T, Ishikawa K (2006) Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: activity toward crystalline chitin. Biosci Biotechnol Biochem 70:1696-1701. doi: 10.1271/bbb.60031
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1696-1701
    • Oku, T.1    Ishikawa, K.2
  • 23
    • 24044553899 scopus 로고    scopus 로고
    • Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp strain O-7
    • 10.1111/j.1365-2672.2005.02630.x 16108796 10.1111/j.1365-2672.2005.02630.x
    • Orikoshi H, Nakayama S, Hanato C, Miyamoto K, Tsujibo H (2005) Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp strain O-7. J Appl Microbiol 99:551-557. doi: 10.1111/j.1365-2672.2005.02630.x
    • (2005) J Appl Microbiol , vol.99 , pp. 551-557
    • Orikoshi, H.1    Nakayama, S.2    Hanato, C.3    Miyamoto, K.4    Tsujibo, H.5
  • 24
    • 0000549004 scopus 로고
    • Halobacterium mediterranei spec, nov., a new carbohydrate-utilizing extreme halophile
    • 10.1016/S0723-2020(83)80021-6 23194735 10.1016/S0723-2020(83)80021-6
    • Rodriguez-Valera F, Juez G, Kushner DJ (1983) Halobacterium mediterranei spec, nov., a new carbohydrate-utilizing extreme halophile. Syst Appl Microbiol 4:369-381. doi: 10.1016/S0723-2020(83)80021-6
    • (1983) Syst Appl Microbiol , vol.4 , pp. 369-381
    • Rodriguez-Valera, F.1    Juez, G.2    Kushner, D.J.3
  • 26
    • 76749113742 scopus 로고    scopus 로고
    • Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste
    • 10.1016/j.biortech.2010.01.036 20133129 10.1016/j.biortech.2010.01.036
    • Songsiriritthigul C, Lapboonrueng S, Pechsrichuang P, Pesatcha P, Yamabhai M (2010) Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste. Bioresour Technol 101:4096-4103. doi: 10.1016/j.biortech.2010.01.036
    • (2010) Bioresour Technol , vol.101 , pp. 4096-4103
    • Songsiriritthigul, C.1    Lapboonrueng, S.2    Pechsrichuang, P.3    Pesatcha, P.4    Yamabhai, M.5
  • 27
    • 84859479892 scopus 로고    scopus 로고
    • First crenarchaeal chitinase found in Sulfolobus tokodaii
    • 10.1016/j.micres.2011.11.001 22154063 10.1016/j.micres.2011.11.001
    • Staufenberger T, Imhoff JF, Labes A (2012) First crenarchaeal chitinase found in Sulfolobus tokodaii. Microbiol Res 167:262-269. doi: 10.1016/j.micres.2011.11.001
    • (2012) Microbiol Res , vol.167 , pp. 262-269
    • Staufenberger, T.1    Imhoff, J.F.2    Labes, A.3
  • 28
    • 0032728411 scopus 로고    scopus 로고
    • A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • 91726 10583986
    • Tanaka T, Fujiwara S, Nishikori S, Fukui T, Takagi M, Imanaka T (1999) A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. Appl Environ Microbiol 65:5338-5344
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5338-5344
    • Tanaka, T.1    Fujiwara, S.2    Nishikori, S.3    Fukui, T.4    Takagi, M.5    Imanaka, T.6
  • 29
    • 3142721163 scopus 로고    scopus 로고
    • Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • 10.1074/jbc.M314187200 15136574 10.1074/jbc.M314187200
    • Tanaka T, Fukui T, Fujiwara S, Atomi H, Imanaka T (2004) Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem 279:30021-30027. doi: 10.1074/jbc.M314187200
    • (2004) J Biol Chem , vol.279 , pp. 30021-30027
    • Tanaka, T.1    Fukui, T.2    Fujiwara, S.3    Atomi, H.4    Imanaka, T.5
  • 30
    • 0035929579 scopus 로고    scopus 로고
    • Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • 10.1074/jbc.M105919200 11468293 10.1074/jbc.M105919200
    • Tanaka T, Fukui T, Imanaka T (2001) Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem 276:35629-35635. doi: 10.1074/jbc.M105919200
    • (2001) J Biol Chem , vol.276 , pp. 35629-35635
    • Tanaka, T.1    Fukui, T.2    Imanaka, T.3
  • 31
    • 77953183572 scopus 로고    scopus 로고
    • Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus - The role of conserved residues in the active site
    • 10.1111/j.1742-464X.2010.07685.x 20553502 10.1111/j.1742-4658.2010.07685.x
    • Tsuji H, Nishimura S, Inui T, Kado Y, Ishikawa K, Nakamura T, Uegaki K (2010) Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus - the role of conserved residues in the active site. FEBS J 277:2683-2695. doi: 10.1111/j.1742-464X.2010.07685.x
    • (2010) FEBS J , vol.277 , pp. 2683-2695
    • Tsuji, H.1    Nishimura, S.2    Inui, T.3    Kado, Y.4    Ishikawa, K.5    Nakamura, T.6    Uegaki, K.7
  • 32
    • 77957727454 scopus 로고    scopus 로고
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
    • 10.1126/science.1192231 20929773 10.1126/science.1192231
    • Vaaje-Kolstad G, Westereng B, Horn SJ, Liu Z, Zhai H, Sørlie M, Eijsink VG (2010) An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330:219-222. doi: 10.1126/science.1192231
    • (2010) Science , vol.330 , pp. 219-222
    • Vaaje-Kolstad, G.1    Westereng, B.2    Horn, S.J.3    Liu, Z.4    Zhai, H.5    Sørlie, M.6    Eijsink, V.G.7
  • 33
    • 84856349841 scopus 로고    scopus 로고
    • Characterization of recombinant family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum strain NRC-1
    • Yoshinobu H, Motosuke S, Keita O, Rie Y, Kimiko E, Toshiaki F, Satoshi N (2006) Characterization of recombinant family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum strain NRC-1. Chitin Chitosan Res 12:201
    • (2006) Chitin Chitosan Res , vol.12 , pp. 201
    • Yoshinobu, H.1    Motosuke, S.2    Keita, O.3    Rie, Y.4    Kimiko, E.5    Toshiaki, F.6    Satoshi, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.