Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon “Ferroplasma acidarmanus” Fer1

Jackson, Brian R.; Noble, Catherine; Lavesa-Curto, Manuel; Bond, Philip L.; Bowater, Richard P.

doi:10.1007/s00792-006-0041-2

Cited by 15 publications

(13 citation statements)

References 56 publications

(142 reference statements)

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“…While the glucosidase and other enzymes from F. acidiphilum have a pH optima ranging from 2 to 3, F. acidarmanus DNA ligase prefers a more neutral environment. It has optimal nick joining activity at pH 6-7, which is similar to DNA ligases from nonacidophiles [60, 61]. This begs the question why some intracellular acidophilic enzymes have such a low pH optima while others, like the DNA ligase, do not.…”

Section: Acidophilic Proteinsmentioning

confidence: 99%

“…This begs the question why some intracellular acidophilic enzymes have such a low pH optima while others, like the DNA ligase, do not. The answer could be related to the substrate of the enzyme; DNA has decreased stability at acidic pH [60, 61]. Therefore, it would be disadvantageous for the F. acidarmanus DNA ligase to be optimally active at a low pH.…”

Section: Acidophilic Proteinsmentioning

confidence: 99%

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Protein Adaptations in Archaeal Extremophiles

Reed

Lewis

Trejo

et al. 2013

Archaea

247

174

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Extremophiles, especially those in Archaea, have a myriad of adaptations that keep their cellular proteins stable and active under the extreme conditions in which they live. Rather than having one basic set of adaptations that works for all environments, Archaea have evolved separate protein features that are customized for each environment. We categorized the Archaea into three general groups to describe what is known about their protein adaptations: thermophilic, psychrophilic, and halophilic. Thermophilic proteins tend to have a prominent hydrophobic core and increased electrostatic interactions to maintain activity at high temperatures. Psychrophilic proteins have a reduced hydrophobic core and a less charged protein surface to maintain flexibility and activity under cold temperatures. Halophilic proteins are characterized by increased negative surface charge due to increased acidic amino acid content and peptide insertions, which compensates for the extreme ionic conditions. While acidophiles, alkaliphiles, and piezophiles are their own class of Archaea, their protein adaptations toward pH and pressure are less discernible. By understanding the protein adaptations used by archaeal extremophiles, we hope to be able to engineer and utilize proteins for industrial, environmental, and biotechnological applications where function in extreme conditions is required for activity.

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Section: Acidophilic Proteinsmentioning

confidence: 99%

Section: Acidophilic Proteinsmentioning

confidence: 99%

Protein Adaptations in Archaeal Extremophiles

Reed

Lewis

Trejo

et al. 2013

Archaea

247

174

View full text Add to dashboard Cite

show abstract

“…Enzymes from acidophiles possess stability in acidic milieus and are active at pH low. Extremozymes from acidophiles possess a great potential for biotechnological and industrial applications especially in biofuel and ethanol production [19]. Nevertheless, the adaptation of some acidiphilic enzymes has not been clearly understood [20].…”

Section: Enzymes Produced By Acidophilic Alkaliphilic Bacteriamentioning

confidence: 99%

Biotechnological and Industrial Applications of Enzymes Produced by Extremophilic Bacteria. A Mini Review

Dumorné

2018

Preprint

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“…Acidithiobacillus ferrooxidans ATP [165] Aeropyrum pernix ATP ADP [166] Ferroplasma acidarmanus ATP [197] Ferroplasma acidophilum ATP NAD + [165] Methanothermobacterium thermoautotrophicum ATP [198] Picrophilus torridus ATP NAD + [165] Pyrococcus horikoshii ATP [169] Pyrococcus furiosus ATP [170] Staphylothermus marinus ATP ADP [167] Sulfophobococcus zilligii ATP ADP GTP [168] Sulfolobus acidocaldarius ATP [165] Sulfolobus shibatae ATP [199] Thermococcus fumicolans ATP NAD + [163] Thermococcus kodakarensis ATP NAD + [162] Thermococcus sp. ATP NAD + [164] Thermococcus sp.…”

Section: Speciesmentioning

confidence: 99%

Rapid progress of DNA replication studies in Archaea, the third domain of life

Ishino

2012

Sci. China Life Sci.

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Archaea, the third domain of life, are interesting organisms to study from the aspects of molecular and evolutionary biology. Archaeal cells have a unicellular ultrastructure without a nucleus, resembling bacterial cells, but the proteins involved in genetic information processing pathways, including DNA replication, transcription, and translation, share strong similarities with those of Eukaryota. Therefore, archaea provide useful model systems to understand the more complex mechanisms of genetic information processing in eukaryotic cells. Moreover, the hyperthermophilic archaea provide very stable proteins, which are especially useful for the isolation of replisomal multicomplexes, to analyze their structures and functions. This review focuses on the history, current status, and future directions of archaeal DNA replication studies.

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Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon “Ferroplasma acidarmanus” Fer1

Cited by 15 publications

References 56 publications

Protein Adaptations in Archaeal Extremophiles

Protein Adaptations in Archaeal Extremophiles

Biotechnological and Industrial Applications of Enzymes Produced by Extremophilic Bacteria. A Mini Review

Rapid progress of DNA replication studies in Archaea, the third domain of life

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