Extremophiles : life under extreme conditions最新文献_第10页

Localized melting of duplex DNA by Cdc6/Orc1 at the DNA replication origin in the hyperthermophilic archaeon Pyrococcus furiosus. 在嗜热古细菌furiosus中，Cdc6/Orc1在DNA复制起点处局部熔化双链DNA。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2010-01-01 Epub Date: 2009-09-30 DOI: 10.1007/s00792-009-0284-9

Fujihiko Matsunaga, Kie Takemura, Masaki Akita, Akinori Adachi, Takeshi Yamagami, Yoshizumi Ishino

{"title":"Localized melting of duplex DNA by Cdc6/Orc1 at the DNA replication origin in the hyperthermophilic archaeon Pyrococcus furiosus.","authors":"Fujihiko Matsunaga, Kie Takemura, Masaki Akita, Akinori Adachi, Takeshi Yamagami, Yoshizumi Ishino","doi":"10.1007/s00792-009-0284-9","DOIUrl":"https://doi.org/10.1007/s00792-009-0284-9","url":null,"abstract":"The initiation step is a key process to regulate the frequency of DNA replication. Although recent studies in Archaea defined the origin of DNA replication (oriC) and the Cdc6/Orc1 homolog as an origin recognition protein, the location and mechanism of duplex opening have remained unclear. We have found that Cdc6/Orc1 binds to oriC and unwinds duplex DNA in the hyperthermophilic archaeon Pyrococcus furiosus, by means of a P1 endonuclease assay. A primer extension analysis further revealed that this localized unwinding occurs in the oriC region at a specific site, which is 12-bp long and rich in adenine and thymine. This site is different from the predicted duplex unwinding element (DUE) that we reported previously. We also discovered that Cdc6/Orc1 induces topological changes in supercoiled oriC DNA, and that this process is dependent on the AAA+ domain. These results indicate that topological alterations of oriC DNA by Cdc6/Orc1 introduce a single-stranded region at the 12-mer site, that could possibly serve as an entry point for Mcm helicase.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"21-31"},"PeriodicalIF":2.9,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-009-0284-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40041991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 21

Bacterial dissimilatory MnO(2) reduction at extremely haloalkaline conditions. 在极端卤碱条件下细菌异化MnO(2)还原。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2010-01-01 Epub Date: 2009-09-25 DOI: 10.1007/s00792-009-0283-x

Dimitri Yu Sorokin, G Muyzer

{"title":"Bacterial dissimilatory MnO(2) reduction at extremely haloalkaline conditions.","authors":"Dimitri Yu Sorokin, G Muyzer","doi":"10.1007/s00792-009-0283-x","DOIUrl":"https://doi.org/10.1007/s00792-009-0283-x","url":null,"abstract":"A possibility of dissimilatory MnO(2) reduction at extremely high salt and pH was studied in sediments from hypersaline alkaline lakes in Kulunda Steppe (Altai, Russia). Experiments with anaerobic sediment slurries demonstrated a relatively rapid reduction of colloidal MnO(2) in the presence of acetate and formate as electron donor at in situ conditions (i.e., pH 10 and a salt content from 0.6 to 4 M total Na(+)). All reduced Mn at these conditions remained in the solid phase. A single, stable enrichment culture was obtained from the slurries consistently reducing MnO(2) at pH 10 and 0.6 M total Na(+) with formate. A pure culture of a haloalkaliphilic Mn-reducing bacterium obtained from the positive enrichment was phylogenetically closely related to the anaerobic haloalkaliphilic Bacillus arseniciselenatis isolated from Mono Lake (CA, USA). Bacillus sp. strain AMnr1 was obligately anaerobic, able to grow either by glucose fermentation, or respiring few nonfermentable substrates by using MnO(2) as the electron acceptor. Optimal growth by dissimilatory MnO(2) reduction was achieved with glycerol as electron donor at pH 9.5-10 and salt content between 0.4 and 0.8 M total Na(+).","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"41-6"},"PeriodicalIF":2.9,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-009-0283-x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40036102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 8

"Hot standards" for the thermoacidophilic archaeon Sulfolobus solfataricus. 嗜热嗜酸古菌溶脂硫酸根的“热标准”。

Extremophiles : life under extreme conditions Pub Date : 2010-01-01 Epub Date: 2009-10-04 DOI: 10.1007/s00792-009-0280-0

Melanie Zaparty, Dominik Esser, Susanne Gertig, Patrick Haferkamp, Theresa Kouril, Andrea Manica, Trong K Pham, Julia Reimann, Kerstin Schreiber, Pawel Sierocinski, Daniela Teichmann, Marleen van Wolferen, Mathias von Jan, Patricia Wieloch, Sonja V Albers, Arnold J M Driessen, Hans-Peter Klenk, Christa Schleper, Dietmar Schomburg, John van der Oost, Phillip C Wright, Bettina Siebers

{"title":"\"Hot standards\" for the thermoacidophilic archaeon Sulfolobus solfataricus.","authors":"Melanie Zaparty, Dominik Esser, Susanne Gertig, Patrick Haferkamp, Theresa Kouril, Andrea Manica, Trong K Pham, Julia Reimann, Kerstin Schreiber, Pawel Sierocinski, Daniela Teichmann, Marleen van Wolferen, Mathias von Jan, Patricia Wieloch, Sonja V Albers, Arnold J M Driessen, Hans-Peter Klenk, Christa Schleper, Dietmar Schomburg, John van der Oost, Phillip C Wright, Bettina Siebers","doi":"10.1007/s00792-009-0280-0","DOIUrl":"10.1007/s00792-009-0280-0","url":null,"abstract":"Within the archaea, the thermoacidophilic crenarchaeote Sulfolobus solfataricus has become an important model organism for physiology and biochemistry, comparative and functional genomics, as well as, more recently also for systems biology approaches. Within the Sulfolobus Systems Biology (\"SulfoSYS\")-project the effect of changing growth temperatures on a metabolic network is investigated at the systems level by integrating genomic, transcriptomic, proteomic, metabolomic and enzymatic information for production of a silicon cell-model. The network under investigation is the central carbohydrate metabolism. The generation of high-quality quantitative data, which is critical for the investigation of biological systems and the successful integration of the different datasets, derived for example from high-throughput approaches (e.g., transcriptome or proteome analyses), requires the application and compliance of uniform standard protocols, e.g., for growth and handling of the organism as well as the \"-omics\" approaches. Here, we report on the establishment and implementation of standard operating procedures for the different wet-lab and in silico techniques that are applied within the SulfoSYS-project and that we believe can be useful for future projects on Sulfolobus or (hyper)thermophiles in general. Beside established techniques, it includes new methodologies like strain surveillance, the improved identification of membrane proteins and the application of crenarchaeal metabolomics.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"119-42"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b8/96/792_2009_Article_280.PMC2797409.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40055348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Acidithiobacillus ferrivorans, sp. nov.; facultatively anaerobic, psychrotolerant iron-, and sulfur-oxidizing acidophiles isolated from metal mine-impacted environments. 酸性铁硫杆菌，sp. 11;兼性厌氧、耐寒的铁和硫氧化嗜酸菌，从受金属矿山影响的环境中分离出来。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2010-01-01 Epub Date: 2009-09-29 DOI: 10.1007/s00792-009-0282-y

Kevin B Hallberg, Elena González-Toril, D Barrie Johnson

{"title":"Acidithiobacillus ferrivorans, sp. nov.; facultatively anaerobic, psychrotolerant iron-, and sulfur-oxidizing acidophiles isolated from metal mine-impacted environments.","authors":"Kevin B Hallberg, Elena González-Toril, D Barrie Johnson","doi":"10.1007/s00792-009-0282-y","DOIUrl":"https://doi.org/10.1007/s00792-009-0282-y","url":null,"abstract":"Phenotypic and genotypic analysis was carried out on four iron- and sulfur-oxidizing acidophilic bacteria (the \"NO-37 group\") isolated from different parts of the world. 16S rRNA phylogeny showed that they are highly related to each other, but are less related to the type strain of Acidithiobacillus ferrooxidans. The NO-37 group isolates are obligate chemolithoautotrophs, facultative anaerobes, diazotrophic, and psychrotolerant. They are less tolerant of extremely low pH, and in contrast to At. ferrooxidans (T), all of the NO-37 group isolates are motile. The GC contents of genomic DNA of the NO-37 group isolates were around 56 mol% and the DNA-DNA hybridization value between genomic DNA of isolate NO-37 and At. ferrooxidans (T) was 37%. It also appears that the bacteria of the NO-37 group have a different biochemical mechanism for oxidizing ferrous iron than At. ferrooxidans (T); the gene coding for the archetypal rusticyanin (RusA) was not detected in any of the NO-37 group isolates, rather a gene coding for a homologous protein (RusB) was amplified from three of the four novel isolates. Isolates of the NO-37 group clearly belong to a species that is different to those already recognized in the genus Acidithiobacillus, for which the name Acidithiobacillus ferrivorans is proposed.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"9-19"},"PeriodicalIF":2.9,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-009-0282-y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40041992","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 205

A thermophilic and acid stable family-10 xylanase from the acidophilic fungus Bispora sp. MEY-1. 来自嗜酸真菌双孢菌MEY-1的嗜热和酸稳定的10家族木聚糖酶。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2009-09-01 Epub Date: 2009-08-05 DOI: 10.1007/s00792-009-0272-0

Huiying Luo, Jiang Li, Jun Yang, Hui Wang, Yuhui Yang, Huoqing Huang, Pengjun Shi, Tiezheng Yuan, Yunliu Fan, Bin Yao

{"title":"A thermophilic and acid stable family-10 xylanase from the acidophilic fungus Bispora sp. MEY-1.","authors":"Huiying Luo, Jiang Li, Jun Yang, Hui Wang, Yuhui Yang, Huoqing Huang, Pengjun Shi, Tiezheng Yuan, Yunliu Fan, Bin Yao","doi":"10.1007/s00792-009-0272-0","DOIUrl":"https://doi.org/10.1007/s00792-009-0272-0","url":null,"abstract":"A complete gene, xyl10C, encoding a thermophilic endo-1,4-beta-xylanase (XYL10C), was cloned from the acidophilic fungus Bispora sp. MEY-1 and expressed in Pichia pastoris. XYL10C shares highest nucleotide and amino acid sequence identities of 57.3 and 49.7%, respectively, with a putative xylanase from Aspergillus fumigatus Af293 of glycoside hydrolase family 10. A high expression level in P. pastoris (73,400 U ml(-1)) was achieved in a 3.7-l fermenter. The purified recombinant XYL10C was thermophilic, exhibiting maximum activity at 85 degrees C, which is higher than that reported from any fungal xylanase. The enzyme was also highly thermostable, exhibiting approximately 100% of the initial activity after incubation at 80 degrees C for 60 min and >87% of activity at 90 degrees C for 10 min. The half lives of XYL10C at 80 and 85 degrees C were approximately 45 and 3 h, respectively. It had two activity peaks at pH 3.0 and 4.5-5.0 (maximum), respectively, and was very acid stable, retaining more than 80% activity after incubation at pH 1.5-6.0 for 1 h. The enzyme was resistant to Co(2+), Mn(2+), Cr(3+) and Ag(+). The specific activity of XYL10C for oat spelt xylan was 18,831 U mg(-1). It also had wide substrate specificity and produced simple products (65.1% xylose, 25.0% xylobiose and 9.9% xylan polymer) from oat spelt xylan.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"849-57"},"PeriodicalIF":2.9,"publicationDate":"2009-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-009-0272-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40011306","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 88

Characterization of the smallest dimeric bile salt hydrolase from a thermophile Brevibacillus sp. 嗜热短芽孢杆菌最小二聚体胆盐水解酶的研究。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2009-03-01 Epub Date: 2009-01-14 DOI: 10.1007/s00792-008-0224-0

N Sridevi, Sameer Srivastava, Bashir Mohammad Khan, Asmita Ashutosh Prabhune

{"title":"Characterization of the smallest dimeric bile salt hydrolase from a thermophile Brevibacillus sp.","authors":"N Sridevi, Sameer Srivastava, Bashir Mohammad Khan, Asmita Ashutosh Prabhune","doi":"10.1007/s00792-008-0224-0","DOIUrl":"https://doi.org/10.1007/s00792-008-0224-0","url":null,"abstract":"A thermophilic microorganism producing bile salt hydrolase was isolated from hot water springs, Pali, Maharashtra, India. This microorganism was identified as Brevibacillus sp. by 16S rDNA sequencing. Bile salt hydrolase (BSH) was purified to homogeneity from this thermophilic source using Q-sepharose chromatography and its enzymatic properties were characterized. The subunit molecular mass of the purified enzyme was estimated to be 28 kDa by SDS-PAGE and, 28.2 kDa by MALDI-TOF analysis. The native molecular mass was estimated to be 56 kDa by gel filtration chromatography, indicating the protein to be a homodimer. The pH and temperature optimum for the enzyme catalysis were 9.0 and 60 degrees C, respectively. Even though BSH from Brevibacillus sp. hydrolyzed all of the six major human bile salts, the enzyme preferred glycine conjugated substrates with apparent K(M) and k(cat) values of 3.08 microM and 6.32 x 10(2) s(-1), respectively, for glycodeoxycholic acid. The NH(2)-terminal sequence of the purified enzyme was determined and it did not show any homology with other bacterial bile salt hydrolases. To our knowledge, this is the first report describing the purification of BSH to homogeneity from a thermophilic source.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"363-70"},"PeriodicalIF":2.9,"publicationDate":"2009-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-008-0224-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39990166","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 20

Morphological changes in an acidophilic bacterium induced by heavy metals. 重金属诱导嗜酸细菌的形态变化。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2008-03-01 Epub Date: 2008-01-10 DOI: 10.1007/s00792-007-0128-4

Rajdeep Chakravarty, Pataki C Banerjee

{"title":"Morphological changes in an acidophilic bacterium induced by heavy metals.","authors":"Rajdeep Chakravarty, Pataki C Banerjee","doi":"10.1007/s00792-007-0128-4","DOIUrl":"https://doi.org/10.1007/s00792-007-0128-4","url":null,"abstract":"The Acidiphilium strains inhabit acidic mine regions where they are subjected to occasional environmental stresses such as high and low temperatures, exposure to various heavy metals, etc. Change in morphology is one of the strategies that bacteria adopt to cope with environmental stresses; however, no study on this aspect has been reported in the case of Acidiphilium sp. This work is an attempt using the acidophilic heterotrophic bacterium Acidiphilium symbioticum H8. It was observed that the maximum alterations in size occurred when the bacterium was exposed to sub-inhibitory concentrations of Cu and Cd. Loosely packed coccobacillus-type normal cells formed characteristic chains of coccoidal lenticular shape with constrictions at the junctions between them in the presence of Cd; Cu induced transformation of cells to become round shaped; Ni caused the cells to aggregate, but Zn showed no effect. Respective metal depositions on the cell surface were confirmed by scanning electron microscopy equipped with energy dispersive X-ray analysis. Cell bound Ca2+ ions were replaced by these metal ions and measured by inductively coupled plasma mass spectrometry from the culture filtrate. Cell shape changed only after the addition of sub-inhibitory concentrations of the metals, but in growth inhibitory concentrations it was similar to the normal cells.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"279-84"},"PeriodicalIF":2.9,"publicationDate":"2008-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-007-0128-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41062022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 93

Biochemical characterization of DNA-binding proteins from Pyrobaculum aerophilum and Aeropyrum pernix. 嗜气焦杆菌和茴香酵母dna结合蛋白的生化特性研究。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2008-03-01 Epub Date: 2007-12-07 DOI: 10.1007/s00792-007-0120-z

Christine D Hardy, Patrick K Martin

{"title":"Biochemical characterization of DNA-binding proteins from Pyrobaculum aerophilum and Aeropyrum pernix.","authors":"Christine D Hardy, Patrick K Martin","doi":"10.1007/s00792-007-0120-z","DOIUrl":"https://doi.org/10.1007/s00792-007-0120-z","url":null,"abstract":"Several representatives of the Crenarchaeal branch of the Archaea contain highly abundant, small, positively charged proteins exemplified by the Sso7d protein from Sulfolobus solfataricus. These proteins bind to DNA in a non-sequence-specific manner. Using publicly available genomic sequence information, we identified a second class of small Crenarchaeal DNA-binding proteins represented by the Pyrobaculum aerophilum open reading frame 3192-encoded (Pae3192) protein and its paralogs. We investigated the biochemical properties of the Pae3192 protein and an orthologous protein (Ape1322b) from Aeropyrum pernix in side-by-side experiments with the Sso7d protein. We demonstrate that the recombinant Ape1322b, Pae3192 and Sso7d proteins bind to DNA and that the DNA-protein complexes formed are slightly different for each protein. We show that like Sso7d, Pae3192 constrains negative supercoils in DNA. In addition, we show that all three proteins raise the melting temperature of duplex DNA upon binding. Finally, we present the equilibrium affinity constants and kinetic association constants of each protein for single-stranded and double-stranded DNA.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"235-46"},"PeriodicalIF":2.9,"publicationDate":"2008-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-007-0120-z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

Insights into different dependence of dNTP triphosphohydrolase on metal ion species from intracellular ion concentrations in Thermus thermophilus. 从嗜热热菌胞内离子浓度分析dNTP三磷酸水解酶对金属离子种类的不同依赖性。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2008-03-01 Epub Date: 2007-11-08 DOI: 10.1007/s00792-007-0118-6

Naoyuki Kondo, Takashi Nishikubo, Taisuke Wakamatsu, Hirohito Ishikawa, Noriko Nakagawa, Seiki Kuramitsu, Ryoji Masui

{"title":"Insights into different dependence of dNTP triphosphohydrolase on metal ion species from intracellular ion concentrations in Thermus thermophilus.","authors":"Naoyuki Kondo, Takashi Nishikubo, Taisuke Wakamatsu, Hirohito Ishikawa, Noriko Nakagawa, Seiki Kuramitsu, Ryoji Masui","doi":"10.1007/s00792-007-0118-6","DOIUrl":"https://doi.org/10.1007/s00792-007-0118-6","url":null,"abstract":"Deoxyribonucleoside triphosphate (dNTP) triphosphohydrolase (dNTPase) from Thermus thermophilus HB8 (TTHB8) hydrolyzes wide variety of dNTPs to deoxyribonucleoside and inorganic triphosphate in magnesium-dependent manner. In this paper, we assess the specificity for various metal ions and of the dNTP triphosphohydrolase activity of the dNTPase from TTHB8. Manganese and cobalt ions more effectively induced the activity for dNTPs than magnesium and, unexpectedly, brought about the degradation of single kind of dNTP. Manganese and cobalt concentrations of 10 nM were enough to induce the activity, while magnesium of about 1 mM was required for the induction of the activity. To further evaluate metal ions inherent to dNTPase in TTHB8 cells, we measured intracellular concentrations of major metal ions in TTHB8 cells by inductively coupled plasma emission spectroscopy and compared them with the dependence of metal ion concentration on dNTPase activity. Though cobalt ion was below detectable level, magnesium and manganese ions were detected at sufficient level to induce dNTPase activity. These results suggest that both manganese and magnesium ions are likely to be functional under intracellular condition. In addition, the proposed model of dNTPase activity induced by magnesium and multiple dNTPs was discussed based on the results obtained in this study.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"217-23"},"PeriodicalIF":2.9,"publicationDate":"2008-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-007-0118-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41021899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 20

First characterisation of the active oligomer form of sulfur oxygenase reductase from the bacterium Aquifex aeolicus. 首次表征了从水蛭中提取的硫氧化酶还原酶的活性低聚物形式。

IF 2.9

Extremophiles : life under extreme conditions Pub Date : 2008-03-01 Epub Date: 2007-12-01 DOI: 10.1007/s00792-007-0119-5

Nicolas Pelletier, Gisèle Leroy, Marianne Guiral, Marie-Thérèse Giudici-Orticoni, Corinne Aubert

{"title":"First characterisation of the active oligomer form of sulfur oxygenase reductase from the bacterium Aquifex aeolicus.","authors":"Nicolas Pelletier, Gisèle Leroy, Marianne Guiral, Marie-Thérèse Giudici-Orticoni, Corinne Aubert","doi":"10.1007/s00792-007-0119-5","DOIUrl":"https://doi.org/10.1007/s00792-007-0119-5","url":null,"abstract":"Sulfur oxygenase reductase (SOR) enzyme is responsible for the initial oxidation step of elemental sulfur in archaea. Curiously, Aquifex aeolicus, a hyperthermophilic, chemolithoautotrophic and microaerophilic bacterium, has the SOR-encoding gene in its genome. We showed, for the first time the presence of the SOR enzyme in A. aeolicus, its gene was cloned and recombinantly expressed in Escherichia coli and the protein was purified and characterised. It is a 16 homo-oligomer of approximately 600 kDa that contains iron atoms indispensable for the enzyme activity. The optimal temperature of SOR activity is 80 degrees C and it is inactive at 20 degrees C. Studies of the factors involved in getting the fully active molecule at high temperature show clearly that (1) incubation at high temperature induces more homogeneous form of the enzyme, (2) conformational changes observed at high temperature are required to get the fully active molecule and (3) acquisition of an active conformation induced by the temperature seems to be more important than the subunit number. Differences between A. aeolicus SOR and the archaea SORs are described.","PeriodicalId":288153,"journal":{"name":"Extremophiles : life under extreme conditions","volume":" ","pages":"205-15"},"PeriodicalIF":2.9,"publicationDate":"2008-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00792-007-0119-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41055242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 24