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Purification, cDNA cloning, and characterization of plant chitinase with a novel domain combination from lycophyte Selaginella doederleinii.
Biosci Biotechnol Biochem 2018; 82(10):1742-1752BB

Abstract

Chitinase-A from a lycophyte Selaginella doederleinii (SdChiA), having molecular mass of 53 kDa, was purified to homogeneity by column chromatography. The cDNA encoding SdChiA was cloned by rapid amplification of cDNA ends and polymerase chain reaction. It consisted of 1477 nucleotides and its open reading frame encoded a polypeptide of 467 amino acid residues. The deduced amino acid sequence indicated that SdChiA consisted of two N-terminal chitin-binding domains and a C-terminal plant class V chitinase catalytic domain, belonging to the carbohydrate-binding module family 18 (CBM18) and glycoside hydrolase family 18 (GH18), respectively. SdChiA had chitin-binding ability. The time-dependent cleavage pattern of (GlcNAc)4 by SdChiA showed that SdChiA specifically recognizes the β-anomer in the + 2 subsite of the substrate (GlcNAc)4 and cleaves the glycoside bond at the center of the substrate. This is the first report of the occurrence of a family 18 chitinase containing CBM18 chitin-binding domains.

ABBREVIATIONS

AtChiC: Arabidopsis thaliana class V chitinase; CBB: Coomassie brilliant blue R250; CBM: carbohydrate binding module family; CrChi-A: Cycas revolute chitinase-A; EaChiA: Equisetum arvense chitinase-A; GH: glycoside hydrolase family, GlxChi-B: gazyumaru latex chitinase-B; GlcNAc: N-acetylglucosamine; HPLC: high performance liquid chromatography; LysM; lysin motif; MtNFH1: Medicago truncatula ecotypes R108-1 chitinase; NCBI: national center for biotechnology information; NF: nodulation factor; NtChiV: Nicotiana tabacum class V chitinase; PCR: polymerase chain reaction; PrChi-A: Pteris ryukyuensis chitinase-A; RACE: rapid amplification of cDNA ends; SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SdChiA: Selaginella doederleinii chitinase-A.

Authors+Show Affiliations

a Graduate School of Agricultural Science , Kagoshima University , Kagoshima , Japan. b Department of Bioscience and Biotechnology , University of the Ryukyus , Okinawa , Japan.a Graduate School of Agricultural Science , Kagoshima University , Kagoshima , Japan. b Department of Bioscience and Biotechnology , University of the Ryukyus , Okinawa , Japan.b Department of Bioscience and Biotechnology , University of the Ryukyus , Okinawa , Japan.a Graduate School of Agricultural Science , Kagoshima University , Kagoshima , Japan. b Department of Bioscience and Biotechnology , University of the Ryukyus , Okinawa , Japan.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

29966504

Citation

Kuba, Yumani, et al. "Purification, cDNA Cloning, and Characterization of Plant Chitinase With a Novel Domain Combination From Lycophyte Selaginella Doederleinii." Bioscience, Biotechnology, and Biochemistry, vol. 82, no. 10, 2018, pp. 1742-1752.
Kuba Y, Takashima T, Uechi K, et al. Purification, cDNA cloning, and characterization of plant chitinase with a novel domain combination from lycophyte Selaginella doederleinii. Biosci Biotechnol Biochem. 2018;82(10):1742-1752.
Kuba, Y., Takashima, T., Uechi, K., & Taira, T. (2018). Purification, cDNA cloning, and characterization of plant chitinase with a novel domain combination from lycophyte Selaginella doederleinii. Bioscience, Biotechnology, and Biochemistry, 82(10), pp. 1742-1752. doi:10.1080/09168451.2018.1491285.
Kuba Y, et al. Purification, cDNA Cloning, and Characterization of Plant Chitinase With a Novel Domain Combination From Lycophyte Selaginella Doederleinii. Biosci Biotechnol Biochem. 2018;82(10):1742-1752. PubMed PMID: 29966504.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, cDNA cloning, and characterization of plant chitinase with a novel domain combination from lycophyte Selaginella doederleinii. AU - Kuba,Yumani, AU - Takashima,Tomoya, AU - Uechi,Keiko, AU - Taira,Toki, Y1 - 2018/07/02/ PY - 2018/7/4/pubmed PY - 2018/11/2/medline PY - 2018/7/4/entrez KW - Chitin-binding domain KW - family 18 chitinase KW - lycophyte KW - plant class V chitinase KW - β-anomer SP - 1742 EP - 1752 JF - Bioscience, biotechnology, and biochemistry JO - Biosci. Biotechnol. Biochem. VL - 82 IS - 10 N2 - : Chitinase-A from a lycophyte Selaginella doederleinii (SdChiA), having molecular mass of 53 kDa, was purified to homogeneity by column chromatography. The cDNA encoding SdChiA was cloned by rapid amplification of cDNA ends and polymerase chain reaction. It consisted of 1477 nucleotides and its open reading frame encoded a polypeptide of 467 amino acid residues. The deduced amino acid sequence indicated that SdChiA consisted of two N-terminal chitin-binding domains and a C-terminal plant class V chitinase catalytic domain, belonging to the carbohydrate-binding module family 18 (CBM18) and glycoside hydrolase family 18 (GH18), respectively. SdChiA had chitin-binding ability. The time-dependent cleavage pattern of (GlcNAc)4 by SdChiA showed that SdChiA specifically recognizes the β-anomer in the + 2 subsite of the substrate (GlcNAc)4 and cleaves the glycoside bond at the center of the substrate. This is the first report of the occurrence of a family 18 chitinase containing CBM18 chitin-binding domains. ABBREVIATIONS: AtChiC: Arabidopsis thaliana class V chitinase; CBB: Coomassie brilliant blue R250; CBM: carbohydrate binding module family; CrChi-A: Cycas revolute chitinase-A; EaChiA: Equisetum arvense chitinase-A; GH: glycoside hydrolase family, GlxChi-B: gazyumaru latex chitinase-B; GlcNAc: N-acetylglucosamine; HPLC: high performance liquid chromatography; LysM; lysin motif; MtNFH1: Medicago truncatula ecotypes R108-1 chitinase; NCBI: national center for biotechnology information; NF: nodulation factor; NtChiV: Nicotiana tabacum class V chitinase; PCR: polymerase chain reaction; PrChi-A: Pteris ryukyuensis chitinase-A; RACE: rapid amplification of cDNA ends; SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SdChiA: Selaginella doederleinii chitinase-A. SN - 1347-6947 UR - https://www.unboundmedicine.com/medline/citation/29966504/Purification,_cDNA_cloning,_and_characterization_of_plant_chitinase_with_a_novel_domain_combination_from_lycophyte_Selaginella_doederleinii L2 - http://www.tandfonline.com/doi/full/10.1080/09168451.2018.1491285 DB - PRIME DP - Unbound Medicine ER -