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Saci_1816: A Trehalase that Catalyzes Trehalose Degradation in the Thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius.
J Microbiol Biotechnol 2018; 28(6):909-916JM

Abstract

Previously, a cytosolic trehalase (TreH) from the hyperthermophilic archaeon Sulfolobus acidocaldarius was reported; however, the gene responsible for the trehalase activity was not identified. Two genes, saci_1816 and saci_1250, that encode the glycoside hydrolase family 15 type glucoamylase-like proteins in S. acidocaldarius were targeted and expressed in Escherichia coli, and their abilities to hydrolyze trehalose were examined. Recombinant Saci_1816 hydrolyzed trehalose exclusively without any help from a cofactor. The mass spectrometric analysis of partially purified native TreH also confirmed that Saci_1816 was involved in proteins exhibiting trehalase activity. Optimal trehalose hydrolysis activity of the recombinant Saci_1816 was observed at pH 4.0 and 60°C. The pH dependence of the recombinant enzyme was similar to that of the native enzyme, but its optimal temperature was 20-25°C lower, and its thermostability was also slightly reduced. From the biochemical and structural results, Saci_1816 was identified as a trehalase responsible for trehalose degradation in S. acidocaldarius. Identification of the treH gene confirms that the degradation of trehalose in Sulfolobus species occurs via the TreH pathway.

Authors+Show Affiliations

Department of Microbiology, College of Natural Sciences, Pusan National University, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, Busan 46241, Republic of Korea. Microbiological Resource Research Institute, Pusan National University, Busan 46241, Republic of Korea.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

29642287

Citation

Lee, Junho, et al. "Saci_1816: a Trehalase That Catalyzes Trehalose Degradation in the Thermoacidophilic Crenarchaeon Sulfolobus Acidocaldarius." Journal of Microbiology and Biotechnology, vol. 28, no. 6, 2018, pp. 909-916.
Lee J, Lee A, Moon K, et al. Saci_1816: A Trehalase that Catalyzes Trehalose Degradation in the Thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius. J Microbiol Biotechnol. 2018;28(6):909-916.
Lee, J., Lee, A., Moon, K., Choi, K. H., & Cha, J. (2018). Saci_1816: A Trehalase that Catalyzes Trehalose Degradation in the Thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius. Journal of Microbiology and Biotechnology, 28(6), pp. 909-916. doi:10.4014/jmb.1802.02038.
Lee J, et al. Saci_1816: a Trehalase That Catalyzes Trehalose Degradation in the Thermoacidophilic Crenarchaeon Sulfolobus Acidocaldarius. J Microbiol Biotechnol. 2018 Jun 28;28(6):909-916. PubMed PMID: 29642287.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Saci_1816: A Trehalase that Catalyzes Trehalose Degradation in the Thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius. AU - Lee,Junho, AU - Lee,Areum, AU - Moon,Keumok, AU - Choi,Kyoung-Hwa, AU - Cha,Jaeho, PY - 2018/4/12/pubmed PY - 2018/10/17/medline PY - 2018/4/12/entrez KW - Glycoside hydrolase family 15 KW - Sulfolobus acidocaldarius KW - trehalase KW - trehalose SP - 909 EP - 916 JF - Journal of microbiology and biotechnology JO - J. Microbiol. Biotechnol. VL - 28 IS - 6 N2 - Previously, a cytosolic trehalase (TreH) from the hyperthermophilic archaeon Sulfolobus acidocaldarius was reported; however, the gene responsible for the trehalase activity was not identified. Two genes, saci_1816 and saci_1250, that encode the glycoside hydrolase family 15 type glucoamylase-like proteins in S. acidocaldarius were targeted and expressed in Escherichia coli, and their abilities to hydrolyze trehalose were examined. Recombinant Saci_1816 hydrolyzed trehalose exclusively without any help from a cofactor. The mass spectrometric analysis of partially purified native TreH also confirmed that Saci_1816 was involved in proteins exhibiting trehalase activity. Optimal trehalose hydrolysis activity of the recombinant Saci_1816 was observed at pH 4.0 and 60°C. The pH dependence of the recombinant enzyme was similar to that of the native enzyme, but its optimal temperature was 20-25°C lower, and its thermostability was also slightly reduced. From the biochemical and structural results, Saci_1816 was identified as a trehalase responsible for trehalose degradation in S. acidocaldarius. Identification of the treH gene confirms that the degradation of trehalose in Sulfolobus species occurs via the TreH pathway. SN - 1738-8872 UR - https://www.unboundmedicine.com/medline/citation/29642287/Saci_1816:_A_Trehalase_that_Catalyzes_Trehalose_Degradation_in_the_Thermoacidophilic_Crenarchaeon_Sulfolobus_acidocaldarius_ L2 - http://www.jmb.or.kr/journal/viewJournal.html?doi=10.4014/jmb.1802.02038 DB - PRIME DP - Unbound Medicine ER -