Journal of Microbiology

Journal Article

Growth of cyanobacterial soil crusts during diurnal freeze-thaw cycles: Steven K. Schmidt , Lara Vimercati; J. Microbiol. 2019;57(4):243-251. Published online February 5, 2019; DOI: https://doi.org/10.1007/s12275-019-8359-5

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Various Nostoc spp. and related cyanobacteria are able to survive extreme temperatures and are among the most successful colonists of high-elevation sites being exposed due to glacial retreat. It is unclear, however, if cyanobacteria can grow during the extreme freeze-thaw cycles that occur on a yearround basis at high-elevation, peri-glacial sites or if they only grow during the rare periods when freeze-thaw cycles do not occur. We conducted several experiments to determine if cyanobacteria that form biological soil crusts (BSCs) at highelevation sites (> 5,000 m.a.s.l.) in the Andes can grow during diurnal freeze-thaw cycles on a par with those that occur in the field. Here we show that a soil crust that had been frozen at -20°C for five years was able to increase from 40% to 100% soil coverage during a 45-day incubation during which the soil temperature cycled between -12°C and 26°C every day. In a second, experiment an undeveloped soil with no visible BSCs showed a statistically significant shift in the bacterial community from one containing few cyanobacterial sequences (8% of sequences) to one dominated (27%) by Nostoc, Microcoleus, and Leptolyngbya phylotypes during a 77-day incubation with daily freeze-thaw cycles. In addition, counts of spherical Nostoc-like colonies increased significantly on the soil surface during the experiment, especially in microcosms receiving phosphorus. Taken together these results show that freeze-thaw cycles alone do not limit the growth of BSCs in high-elevation soils, and provide new insight into how life is able to thrive in one of the most extreme terrestrial environments on Earth.

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Review

MINIREVIEW] Global transcriptional regulator TrmB family members in prokaryotes: Minwook Kim , Soyoung Park , Sung-Jae Lee; J. Microbiol. 2016;54(10):639-645. Published online September 30, 2016; DOI: https://doi.org/10.1007/s12275-016-6362-7

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Abstract

Members of the TrmB family act as global transcriptional regulators for the activation or repression of sugar ABC transporters and central sugar metabolic pathways, including glycolytic, gluconeogenic, and other metabolic pathways, and also as chromosomal stabilizers in archaea. As a relatively newly classified transcriptional regulator family, there is limited experimental evidence for their role in Thermococcales, halophilic archaeon Halobacterium salinarum NRC1, and crenarchaea Sulfolobus strains, despite being one of the extending protein families in archaea. Recently, the protein structures of Pyrococcus furiosus TrmB and TrmBL2 were solved, and the transcriptomic data uncovered by microarray and ChIP-Seq were published. In the present review, recent evidence of the functional roles of TrmB family members in archaea is explained and extended to bacteria.

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

Cloning and Characterization of Thermostable Esterase from Archaeoglobus fulgidus: Seung-Bum Kim , Wonkyu Lee , Yeon-Woo Ryu; J. Microbiol. 2008;46(1):100-107.; DOI: https://doi.org/10.1007/s12275-007-0185-5

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Abstract: Thermostable esterase gene was cloned (Est-AF) from extremophilic microorganisms, Archaeoglobus fulgidus DSM 4304. The protein analysis result showed that Est-AF is monomer with total 247 amino acids and molecular weight of estimated 27.5 kDa. It also showed repeating units G-X-S-X-G (GHSLG) (residues 86~90) which is reported as active site of known esterases, and the putative catalytic triad composed of Ser88, Asp198 and His226. The esterase activity test with various acyl chain length of ρ-nitrophenol resulted that Est-AF showed highest specific activity with ρ-nitrophenylbutyrate (pNPC4) and rapidly decrease with ρ-nitrophenyl ester contain more than 8 carbon chain. These results represent that cloned enzyme is verified as a carboxylesterase but not a lipase because esterase activity is decreased with ρ-nitrophenyl ester contains more than 8 carbon chains but lipase activity does not affected with carbon chain length. Optimum temperature of esterase reaction with ρ-nitrophenylbutyrate (pNPC4) was 80°C. When ketoprofen ethyl ester was used as a substrate, activity of Est-AF showed the highest value at 70°C, and 10% of activity still remains after 3 h of incubation at 90°C. This result represents Est-AF has high thermostability with comparison of other esterases that have been reported. However, Est-AF showed low enantioselectivity with ketoprofen ethyl ester. Optimum pH of Est-AF is between pH 7.0 and pH 8.0. Km value of ketoprofen ethyl ester is 1.6 mM and, Vmax is 1.7 μmole/mg protein/min. Est-AF showed similar substrate affinity but slower reaction with ketoprofen ethyl ester compare with esterase from mesophilic strain P. fluorescens.

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