Extremophiles (EXTREMOPHILES)

Publisher: Springer Verlag

Journal description

Extremophiles features original research articles reviews and method papers on the biology molecular biology structure function and applications of life at high or low temperature pressure acidity alkalinity salinity or oxygen concentration; or in the presence of organic solvents heavy metals normally toxic substances radiation or host defense mechanisms. Fields covered: molecular biology biodiversity genetics macromolecular structure development growth biotechnology / fermentation technology ultrastructure biotransformation metabolism enzymology biomembranes bioenergetics physiology cell biology symbiosis ecology bioremediation methodologies evolution isolation phylogeny taxonomy

Current impact factor: 2.17

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 2.174
2012 Impact Factor 2.203
2011 Impact Factor 2.941
2010 Impact Factor 2.16
2009 Impact Factor 2
2008 Impact Factor 1.782
2007 Impact Factor 2.317
2006 Impact Factor 1.921
2005 Impact Factor 2.125
2004 Impact Factor 1.897
2003 Impact Factor 1.955
2002 Impact Factor 2.165
2001 Impact Factor 2.291
2000 Impact Factor 2.688
1999 Impact Factor 3.133
1998 Impact Factor 2.593
1997 Impact Factor

Impact factor over time

Impact factor

Additional details

5-year impact 2.46
Cited half-life 6.50
Immediacy index 0.44
Eigenfactor 0.01
Article influence 0.76
Website Extremophiles website
Other titles Extremophiles (Online)
ISSN 1431-0651
OCLC 42900820
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Springer Verlag

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Author's pre-print on pre-print servers such as arXiv.org
    • Author's post-print on author's personal website immediately
    • Author's post-print on any open access repository after 12 months after publication
    • Publisher's version/PDF cannot be used
    • Published source must be acknowledged
    • Must link to publisher version
    • Set phrase to accompany link to published version (see policy)
    • Articles in some journals can be made Open Access on payment of additional charge
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: The deleterious effects of ionizing radiation are a major concern of the modern world. In the last decades, outstanding interest has been given to developing new therapeutic tools designed for protection against the toxic effects of ionizing radiation. Deinococcus spp. are among the most radioresistant organisms on Earth, being able to survive extreme doses of radiation, 1000-fold higher than most vertebrates. The molecular mechanisms underlying DNA repair and biomolecular protection, which are responsible for the remarkable radioresistance of Deinococcus bacteria, have been a debatable subject for the last 60 years. This paper is focused on the most recent findings regarding the molecular background of radioresistance and on Deinococcus bacteria response to oxidative stress. Novel proteins and genes involved in the highly regulated DNA repair processes, and enzymatic and non- enzymatic antioxidant systems are presented. In addition, a recently proposed mechanism that may contribute to oxidative damage protection in Deinococcus bacteria is discussed. A better understanding of these molecular mechanisms may draw future perspectives for counteracting radiation-related toxicity.
    Extremophiles 06/2015; DOI:10.1007/s00792-015-0759-9
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    ABSTRACT: A total of 33 halophilic protease producers were isolated from different salt samples collected from Emisal salt company at Lake Qarun, Fayoum, Egypt. Of these strains, an extremely halophilic strain that grew optimally at 30 % (w/v) NaCl was characterized and identified as Halobacterium sp. strain HP25 based on 16S rRNA gene sequencing and phenotypic characterization. A halo-alkali-thermophilic protease was purified in three successive steps from the culture supernatant. The purified halophilic protease consisted of a single polypeptide chain with a molecular mass of 21 kDa and was enriched 167-fold to a specific activity of 6350 U mg(-1). The purified enzyme was active over a broad pH range from 6.0 to 11.0, with maximum activity at pH 8.0, exhibited a broad temperature range from 30 to 80 °C with optimum activity at 60 °C, and was active at salt concentrations ranging from 5 to 25 % (w/v), with optimum activity at 17 % NaCl (w/v). The K M and V max values of the purified halophilic protease with casein as a substrate were 523 µg mL(-1) and 2500 µg min(-1) mL(-1), respectively. In addition, this enzyme was stable in the tested organic solvents and laundry detergents such methanol, propanol, butanol, hexane, Persil and Ariel. The unusual properties of this enzyme allow it to be used for various applications, such as the ripening of salted fish. Furthermore, its stability and activity in the presence of organic solvents and detergents also allow the use of this enzyme for further novel applications and as an additive in detergent formulations.
    Extremophiles 05/2015; DOI:10.1007/s00792-015-0752-3
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    ABSTRACT: Psychrophilic microorganisms are cold-adapted with distinct properties from other thermal classes thriving in cold conditions in large areas of the earth's cold environment. Maintenance of functional membranes, evolving cold-adapted enzymes and synthesizing a range of structural features are basic adaptive strategies of psychrophiles. Among the cold-evolved enzymes are the cold-active lipases, a group of microbial lipases with inherent stability-activity-flexibility property that have engaged the interest of researchers over the years. Current knowledge regarding these cold-evolved enzymes in psychrophilic bacteria proves a display of high catalytic efficiency with low thermal stability, which is a differentiating feature with that of their mesophilic and thermophilic counterparts. Improvement strategies of their adaptive structural features have significantly benefited the enzyme industry. Based on their homogeneity and purity, molecular characterizations of these enzymes have been successful and their properties make them unique biocatalysts for various industrial and biotechnological applications. Although, strong association of lipopolysaccharides from Antarctic microorganisms with lipid hydrolases pose a challenge in their purification, heterologous expression of the cold-adapted lipases with affinity tags simplifies purification with higher yield. The review discusses these cold-evolved lipases from bacteria and their peculiar properties, in addition to their potential biotechnological and industrial applications.
    Extremophiles 03/2015; 19(2):235-247. DOI:10.1007/s00792-014-0710-5
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    ABSTRACT: Pristine and oil-contaminated desert soil samples from Kuwait harbored between 10 and 100 cells g(-1) of hydrocarbonoclastic bacteria capable of growth at 50 °C. Enrichment by incubation of moistened soils for 6 months at 50 °C raised those numbers to the magnitude of 10(3) cells g(-1). Most of these organisms were moderately thermophilic and belonged to the genus Bacillus; they grew at 40-50 °C better than at 30 °C. Species belonging to the genera Amycolatopsis, Chelativorans, Isoptericola, Nocardia, Aeribacillus, Aneurinibacillus, Brevibacillus, Geobacillus, Kocuria, Marinobacter and Paenibacillus were also found. This microbial diversity indicates a good potential for hydrocarbon removal in soil at high temperature. Analysis of the same desert soil samples by a culture-independent method (combined, DGGE and 16S rDNA sequencing) revealed dramatically different lists of microorganisms, many of which had been recorded as hydrocarbonoclastic. Many species were more frequent in the oil contaminated than in the pristine soil samples, which may reflect their hydrocarbonoclastic activity in situ. The growth and hydrocarbon consumption potential of all tested isolates were dramatically enhanced by amendment of the cultures with Ca(2+) (up to 2.5 M CaSO4). This enhanced effect was even amplified when in addition 8 % w/v dipicolinic acid was amended. These novel findings are useful in suggesting biotechnologies for waste hydrocarbon remediation at moderately high temperature.
    Extremophiles 02/2015; 19(3). DOI:10.1007/s00792-015-0739-0
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    ABSTRACT: On Saturday 5 July 2014, Wilhelmus Nicolaas Konings (known as Wil Konings), Emeritus Professor of Molecular Microbiology, passed away at the age of 76. He was born and grew up in Maastricht, the Netherlands. He received his Ph.D. from the University of Groningen in 1969. From 1969 until 1971 he worked at the National Institute of Health, Bethesda, as a post-doctoral fellow. In 1971, he was appointed lecturer and in 1980 promoted to professor in Microbiology at the University of Groningen; in 2002 he retired as Professor Emeritus, leaving a legacy of more than 440 scientific papers and 7 patents, and numerous students and post docs who were trained in his laboratory.Wil Konings was an engaging and striking personality, who, from the middle of the seventies, played a prominent role in the field of microbiology and in particular the area of the membrane biology. He was a very talented researcher with an international reputation and stature that fits in the rich tradition of Dutch microbio ...
    Extremophiles 02/2015; 19(2). DOI:10.1007/s00792-015-0736-3
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    ABSTRACT: Halophilic archaea offer a potential source for production of polyhydroxyalkanoates (PHAs). Hence, the experiments were carried out with five extremely halophilic archaeal isolates to determine the highest PHA-producing strain. PHA production of each isolates was separately examined in cheap carbon sources such as corn starch, sucrose, whey, apple, melon and tomato wastes. Corn starch was found to be a fairly effective substrate for PHA production. Among the strains studied here, the strain with the highest capability for PHA biosynthesis was found to be 1KYS1. Phylogenetic analysis based on 16S rRNA gene sequence comparison showed that 1KYS1 closely related to species of the genus Natrinema. The closest phylogenetic similarity was with the strain of Natrinema pallidum JCM 8980 (99 %). PHA content of 1KYS1 was about 53.14 % of the cell dry weight when starch was used as a carbon source. The formation of large and uniform PHA granules was confirmed by transmission electron microscopy and the biopolymer was identified as poly(3-hydroxybutyrate-co-hydroxyvalerate) (PHBV). PHBV produced by 1KYS1 was blended with low molar mass polyethylene glycol (PEG 300) to prepare biocompatible films for drug delivery. Rifampicin was used as a model drug and its release from PHBV films was investigated at pH 7.4, 37 °C. It was found that PHBV films obtained from 1KYS1 were very effective for drug delivery. In conclusion, PHBV of 1KYS1 may have a potential usage in drug delivery applications.
    Extremophiles 02/2015; 19(2). DOI:10.1007/s00792-015-0735-4
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    ABSTRACT: The in vivo functions of Hje and Hjc, two Holliday junction resolvases in Sulfolobus islandicus were investigated. We found that deletion of either hje or hjc had no effect on normal cell growth, while deletion of both hje and hjc is lethal. Although Hjc is the conserved resolvase in all archaea, the hje deletion rather than hjc deletion rendered cells more sensitive to DNA-damaging agents such as hydroxyurea, cisplatin, and methyl methanesulfonate than the wild type (WT). Intriguingly, the sensitivity of Δhje could not be rescued by ectopic expression of Hje from a plasmid and Hje overexpression slowed growth and large cells appeared with more than two genome equivalents. We showed that Hje was maintained at a low level in WT cells. Furthermore, transcriptomic microarray analysis revealed that the abundance of transcripts of many genes including those involved in DNA replication, repair, transcription regulation, and cell division changed drastically in the Hje-overexpressed strain. However, only limited genes were up- or downregulated in the hje deletion strain. Our findings collectively suggest that Hje is the primary resolvase involved in DNA repair and its expression must be tightly controlled in cells.
    Extremophiles 02/2015; 19(2). DOI:10.1007/s00792-015-0734-5
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    ABSTRACT: We identified the non-phosphorylated l-rhamnose metabolic pathway (Rha_NMP) genes that are homologous to those in the thermoacidophilic archaeon Thermoplasma acidophilum in the genome of the thermoacidophilic bacterium Sulfobacillus thermosulfidooxidans. However, unlike previously known 2-keto-3-deoxy-l-rhamnonate (l-KDR) dehydrogenase (KDRDH) which belongs to the short chain dehydrogenase/reductase superfamily, the putative KDRDHs in S. thermosulfidooxidans (Sulth_3557) and T. acidophilum (Ta0749) belong to the medium chain dehydrogenase/reductase (MDR) superfamily. We demonstrated that Sulth_3559 and Sulth_3557 proteins from S. thermosulfidooxidans function as l-rhamnose dehydrogenase and KDRDH, respectively. Sulth_3557 protein is an NAD+-specific KDRDH with optimal temperature and pH of 50 °C and 9.5, respectively. The K m and V max values for l-KDR were 2.0 mM and 12.8 U/mg, respectively. Sulth_3557 also showed weak 2,3-butanediol dehydrogenase activity. Phylogenetic analysis suggests that Sulth_3557 and its homologs form a new subfamily in the MDR superfamily. The results shown in this study imply that thermoacidophilic archaea metabolize l-rhamnose to pyruvate and l-lactate by using the MDR-family KDRDH similarly to that of the thermoacidophilic bacterium S. thermosulfidooxidans.
    Extremophiles 01/2015; 19(2). DOI:10.1007/s00792-015-0731-8
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    ABSTRACT: The effects of salt on the structure, stability, and enzymatic function of a novel dihydrofolate reductase (HjDHFR P1) from a hyperhalophilic archaeon, Haloarcula japonica strain TR-1 living in a Japanese saltern, were studied using ultraviolet absorption, circular dichroism (CD), and fluorescence spectroscopy. HjDHFR P1 had a partial structure at pH 8.0 in the absence of NaCl, and the addition of NaCl (0-500 mM concentration) induced significant structural formation to HjDHFR P1. The addition of NADPH, which is a coenzyme for its catalytic reaction, and lowering the pH from 8 to 6 also induced the same CD change, indicating the formation of the NADPH-binding site in HjDHFR P1. The NaCl dependence of thermal and urea-induced unfolding measurements suggested that protein stability increased depending on NaCl concentration regardless of structural formation, and HjDHFR P1 achieved the same stability as Escherichia coli DHFR at 750 mM NaCl. Halophilic characteristics were also observed for enzymatic function, although its structure had already formed under the conditions that enzymatic activity was measured at due to the presence of NADPH. These results suggest that the halophilic mechanism on structural stability and function was caused by factors other than structural formation, which are suggested to be the contributions of preferential interactions between the protein and salt ions and the specific binding of salt ions.
    Extremophiles 01/2015; 19(2). DOI:10.1007/s00792-015-0732-7
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    ABSTRACT: Copahue is a natural geothermal field (Neuquén province, Argentina) dominated by the Copahue volcano. As a consequence of the sustained volcanic activity, Copahue presents many acidic pools, hot springs and solfataras with different temperature and pH conditions that influence their microbial diversity. The occurrence of microbial biofilms was observed on the surrounding rocks and the borders of the ponds, where water movements and thermal activity are less intense. Microbial biofilms are particular ecological niches within geothermal environments; they present different geochemical conditions from that found in the water of the ponds and hot springs which is reflected in different microbial community structure. The aim of this study is to compare microbial community diversity in the water of ponds and hot springs and in microbial biofilms in the Copahue geothermal field, with particular emphasis on Cyanobacteria and other photosynthetic species that have not been detected before in Copahue. In this study, we report the presence of Cyanobacteria, Chloroflexi and chloroplasts of eukaryotes in the microbial biofilms not detected in the water of the ponds. On the other hand, acidophilic bacteria, the predominant species in the water of moderate temperature ponds, are almost absent in the microbial biofilms in spite of having in some cases similar temperature conditions. Species affiliated with Sulfolobales in the Archaea domain are the predominant microorganism in high temperature ponds and were also detected in the microbial biofilms.
    Extremophiles 01/2015; 19(2). DOI:10.1007/s00792-015-0729-2
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    ABSTRACT: The enzyme 5-phosphoribosyl-1-α-diphosphate (PRPP) synthase (EC catalyses the Mg(2+)-dependent transfer of a diphosphoryl group from ATP to the C1 hydroxyl group of ribose 5-phosphate resulting in the production of PRPP and AMP. A nucleotide sequence specifying Sulfolobus solfataricus PRPP synthase was synthesised in vitro with optimised codon usage for expression in Escherichia coli. Following expression of the gene in E. coli PRPP synthase was purified by heat treatment and ammonium sulphate precipitation and the structure of S. solfataricus PRPP synthase was determined at 2.8 Å resolution. A bent dimer oligomerisation was revealed, which seems to be an abundant feature among PRPP synthases for defining the adenine specificity of the substrate ATP. Molecular replacement was used to determine the S. solfataricus PRPP synthase structure with a monomer subunit of Methanocaldococcus jannaschii PRPP synthase as a search model. The two amino acid sequences share 35 % identity. The resulting asymmetric unit consists of three separated dimers. The protein was co-crystallised in the presence of AMP and ribose 5-phosphate, but in the electron density map of the active site only AMP and a sulphate ion were observed. Sulphate ion, reminiscent of the ammonium sulphate precipitation step of the purification, seems to bind tightly and, therefore, presumably occupies and blocks the ribose 5-phosphate binding site. The activity of S. solfataricus PRPP synthase is independent of phosphate ion.
    Extremophiles 01/2015; 19(2). DOI:10.1007/s00792-014-0726-x