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Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance.
FEMS Microbiol Lett. 2012 Aug; 333(1):46-53.FM

Abstract

Serine hydroxymethyltransferase (SHMT) is a key enzyme in cellular one-carbon pathway and has been studied in many living organisms from bacteria to higher plants and mammals. However, biochemical and molecular characterization of SHMT from photoautotrophic microorganisms remains a challenge. Here, we isolated the SHMT gene from a halotolerant cyanobacterium Aphanothece halophytica (ApSHMT) and expressed it in Escherichia coli. Purified recombinant ApSHMT protein exhibited catalytic reactions for dl-threo-3-phenylserine as well as for l-serine. Catalytic reaction for l-serine was strongly inhibited by NaCl, but not to that level with glycine betaine. Overexpression of ApSHMT in E. coli resulted in the increased accumulation of glycine and serine. Choline and glycine betaine levels were also significantly increased. Under high salinity, the growth rate of ApSHMT-expressing cells was faster compared to its respective control. High salinity also strongly induced the transcript level of ApSHMT in A. halophytica. Our results indicate the importance of a novel pathway; salt-induced ApSHMT increased the level of glycine betaine via serine and choline and conferred the tolerance to salinity stress.

Authors+Show Affiliations

Research Institute of Meijo University, Nagoya, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22587350

Citation

Waditee-Sirisattha, Rungaroon, et al. "Overexpression of Serine Hydroxymethyltransferase From Halotolerant Cyanobacterium in Escherichia Coli Results in Increased Accumulation of Choline Precursors and Enhanced Salinity Tolerance." FEMS Microbiology Letters, vol. 333, no. 1, 2012, pp. 46-53.
Waditee-Sirisattha R, Sittipol D, Tanaka Y, et al. Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance. FEMS Microbiol Lett. 2012;333(1):46-53.
Waditee-Sirisattha, R., Sittipol, D., Tanaka, Y., & Takabe, T. (2012). Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance. FEMS Microbiology Letters, 333(1), 46-53. https://doi.org/10.1111/j.1574-6968.2012.02597.x
Waditee-Sirisattha R, et al. Overexpression of Serine Hydroxymethyltransferase From Halotolerant Cyanobacterium in Escherichia Coli Results in Increased Accumulation of Choline Precursors and Enhanced Salinity Tolerance. FEMS Microbiol Lett. 2012;333(1):46-53. PubMed PMID: 22587350.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance. AU - Waditee-Sirisattha,Rungaroon, AU - Sittipol,Daungjai, AU - Tanaka,Yoshito, AU - Takabe,Teruhiro, Y1 - 2012/06/11/ PY - 2012/03/24/received PY - 2012/05/09/revised PY - 2012/05/11/accepted PY - 2012/5/17/entrez PY - 2012/5/17/pubmed PY - 2012/11/9/medline SP - 46 EP - 53 JF - FEMS microbiology letters JO - FEMS Microbiol. Lett. VL - 333 IS - 1 N2 - Serine hydroxymethyltransferase (SHMT) is a key enzyme in cellular one-carbon pathway and has been studied in many living organisms from bacteria to higher plants and mammals. However, biochemical and molecular characterization of SHMT from photoautotrophic microorganisms remains a challenge. Here, we isolated the SHMT gene from a halotolerant cyanobacterium Aphanothece halophytica (ApSHMT) and expressed it in Escherichia coli. Purified recombinant ApSHMT protein exhibited catalytic reactions for dl-threo-3-phenylserine as well as for l-serine. Catalytic reaction for l-serine was strongly inhibited by NaCl, but not to that level with glycine betaine. Overexpression of ApSHMT in E. coli resulted in the increased accumulation of glycine and serine. Choline and glycine betaine levels were also significantly increased. Under high salinity, the growth rate of ApSHMT-expressing cells was faster compared to its respective control. High salinity also strongly induced the transcript level of ApSHMT in A. halophytica. Our results indicate the importance of a novel pathway; salt-induced ApSHMT increased the level of glycine betaine via serine and choline and conferred the tolerance to salinity stress. SN - 1574-6968 UR - https://www.unboundmedicine.com/medline/citation/22587350/Overexpression_of_serine_hydroxymethyltransferase_from_halotolerant_cyanobacterium_in_Escherichia_coli_results_in_increased_accumulation_of_choline_precursors_and_enhanced_salinity_tolerance_ L2 - https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.2012.02597.x DB - PRIME DP - Unbound Medicine ER -