Sulfolobus solfataricus

Sulfolobus solfataricus is the most studied microorganism from a molecular, genetic, and biochemical point of view for its ability to thrive in extreme environments. It can grow easily in the laboratory, and it can exchange genetic material through processes of transformation, transduction, and conjugation.

The major motivation for sequencing these microorganisms is to study the thermostability of proteins that normally denature at a high temperature. The complete sequence the genome of S. solfataricus was completed in 2001.{{cite journal | vauthors = Charlebois RL, Gaasterland T, Ragan MA, Doolittle WF, Sensen CW | title = The Sulfolobus solfataricus P2 genome project | journal = FEBS Letters | volume = 389 | issue = 1 | pages = 88–91 | date = June 1996 | pmid = 8682213 | doi = 10.1016/s0014-5793(97)81281-1 | bibcode = 1996FEBSL.398R.343. | s2cid = 221414122 }} On a single chromosome, there are 2,992,245 base pairs, which encode 2,977 proteins and copious RNAs. One-third of S. solfataricus encoded proteins have no homologs in other genomes. For the remaining encoded proteins, 40% are specific to Archaea, 12% are shared with Bacteria, and 2.3% are shared with Eukaryote; 33% of these proteins are encoded exclusively in Sulfolobus. A high number of open reading frames (ORFs) are highly similar in Thermoplasma.

Small nucleolar RNAs (snoRNAs), already present in eukaryotes, have also been identified in S. solfataricus and S. acidolcaldarius. They are already known for the role they play in post-transcriptional modifications and removal of introns from ribosomal RNA in Eukaryote.{{cite journal | vauthors = Omer AD, Lowe TM, Russell AG, Ebhardt H, Eddy SR, Dennis PP | title = Homologs of small nucleolar RNAs in Archaea | journal = Science | volume = 288 | issue = 5465 | pages = 517–22 | date = April 2000 | pmid = 10775111 | doi = 10.1126/science.288.5465.517 | bibcode = 2000Sci...288..517O | s2cid = 15552500 }}

The genome of Sulfolobus is characterized by the presence of short tandem repeats, insertion and repetitive elements. It has a wide range of diversity with 200 different insertion sequence elements.

The stabilization of the DNA's structure against denaturation, in the Archaea, is due to the presence of a particular thermophilic enzyme, reverse gyrase. It was discovered in hyper-thermophilic and thermophilic Archaea and Bacteria. There are two genes in Sulfolobus that each encode a reverse gyrase.{{cite journal | vauthors = Couturier M, Bizard AH, Garnier F, Nadal M | title = Insight into the cellular involvement of the two reverse gyrases from the hyperthermophilic archaeon Sulfolobus solfataricus | journal = BMC Molecular Biology | volume = 15 | issue = 1 | pages = 18 | date = September 2014 | pmid = 25200003 | pmc = 4183072 | doi = 10.1186/1471-2199-15-18 | doi-access = free }} It is defined as an atypical DNA topoisomerase and the basic activity consists of the production of positive supercoils in a closed circular DNA. Positive supercoiling is important to prevent the formation of open complexes. Reverse gyrases are composed of two domains: the first one is the helicase and second one is the topoisomerase I. A possible role of reverse gyrase could be the use of positive supercoiling to assemble chromatin-like structures.{{cite journal | vauthors = Déclais AC, Marsault J, Confalonieri F, de La Tour CB, Duguet M | title = Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling | journal = The Journal of Biological Chemistry | volume = 275 | issue = 26 | pages = 19498–504 | date = June 2000 | pmid = 10748189 | doi = 10.1074/jbc.m910091199 | doi-access = free }} In 1997, scientists discovered another important feature of Sulfolobus: a type-II topoisomerase, called TopoVI, whose A subunit is homologous to the meiotic recombination factor, Spo11, which plays a predominant role in the initiation of meiotic recombination in all Eukaryotes.{{cite journal | vauthors = Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P | title = An atypical topoisomerase II from Archaea with implications for meiotic recombination | journal = Nature | volume = 386 | issue = 6623 | pages = 414–7 | date = March 1997 | pmid = 9121560 | doi = 10.1038/386414a0 | bibcode = 1997Natur.386..414B | s2cid = 4327493 }}{{cite journal | vauthors = Forterre P, Bergerat A, Lopez-Garcia P | title = The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea | journal = FEMS Microbiology Reviews | volume = 18 | issue = 2–3 | pages = 237–48 | date = May 1996 | pmid = 8639331 | doi = 10.1111/j.1574-6976.1996.tb00240.x | doi-access = free }}

S. solfataricus is composed of three topoisomerases of type I, TopA and two reverse gyrases, TopR1 and TopR2, and one topoisomerase of type II, TopoVI.{{cite journal | vauthors = Couturier M, Gadelle D, Forterre P, Nadal M, Garnier F | title = The reverse gyrase TopR1 is responsible for the homeostatic control of DNA supercoiling in the hyperthermophilic archaeon Sulfolobus solfataricus | journal = Molecular Microbiology | date = November 2019 | volume = 113 | issue = 2 | pages = 356–368 | pmid = 31713907 | doi = 10.1111/mmi.14424 | s2cid = 207945754 | doi-access = free }}

In the phylum Thermoproteota, there are three proteins that bind to the minor groove of DNA-like histones, Alba, Cren7, and Sso7d, that are modified after the translation process. These histones are small and have been found in several strains of Sulfolobus, but not in other genomes. Chromatin protein in Sulfolobus represent 1-5% of the total genome; they can have both structural and regulatory functions and look like human HMG-box proteins because of their influence on genomes, expression, stability, and epigenetic processes.{{cite journal | vauthors = Malarkey CS, Churchill ME | title = The high mobility group box: the ultimate utility player of a cell | journal = Trends in Biochemical Sciences | volume = 37 | issue = 12 | pages = 553–62 | date = December 2012 | pmid = 23153957 | pmc = 4437563 | doi = 10.1016/j.tibs.2012.09.003 }} In species lacking histones, they can be acetylated and methylated like eukaryotic histones.{{cite journal | vauthors = Payne S, McCarthy S, Johnson T, North E, Blum P | title = Sulfolobus solfataricus | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 115 | issue = 48 | pages = 12271–12276 | date = November 2018 | pmid = 30425171 | pmc = 6275508 | doi = 10.1073/pnas.1808221115 | doi-access = free }}{{cite journal | vauthors = Guagliardi A, Cerchia L, Moracci M, Rossi M | title = The chromosomal protein sso7d of the crenarchaeon Sulfolobus solfataricus rescues aggregated proteins in an ATP hydrolysis-dependent manner | journal = The Journal of Biological Chemistry | volume = 275 | issue = 41 | pages = 31813–8 | date = October 2000 | pmid = 10908560 | doi = 10.1074/jbc.m002122200 | doi-access = free }}{{cite journal | vauthors = Shehi E, Granata V, Del Vecchio P, Barone G, Fusi P, Tortora P, Graziano G | title = Thermal stability and DNA binding activity of a variant form of the Sso7d protein from the archeon Sulfolobus solfataricus truncated at leucine 54 | journal = Biochemistry | volume = 42 | issue = 27 | pages = 8362–8 | date = July 2003 | pmid = 12846585 | doi = 10.1021/bi034520t }}{{cite journal | vauthors = Baumann H, Knapp S, Karshikoff A, Ladenstein R, Härd T | title = DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus | journal = Journal of Molecular Biology | volume = 247 | issue = 5 | pages = 840–6 | date = April 1995 | pmid = 7723036 | doi = 10.1006/jmbi.1995.0184 | doi-access = free }} Sulfolobus strains present different peculiar DNA binding proteins, such as the Sso7d protein family. They stabilize the DNA's structure, preventing denaturation at high temperature and thus promoting annealing above the melting point.{{cite journal | vauthors = Guagliardi A, Napoli A, Rossi M, Ciaramella M | title = Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein | journal = Journal of Molecular Biology | volume = 267 | issue = 4 | pages = 841–8 | date = April 1997 | pmid = 9135116 | doi = 10.1006/jmbi.1996.0873 }}

The major component of Archaea chromatin is represented by Sac10b family protein known as Alba (acetylation lowers binding affinity).{{cite journal | vauthors = Forterre P, Confalonieri F, Knapp S | title = Identification of the gene encoding archeal-specific DNA-binding proteins of the Sac10b family | journal = Molecular Microbiology | volume = 32 | issue = 3 | pages = 669–70 | date = May 1999 | pmid = 10320587 | doi = 10.1046/j.1365-2958.1999.01366.x | s2cid = 28146814 }}{{cite journal | vauthors = Xue H, Guo R, Wen Y, Liu D, Huang L | title = An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion | journal = Journal of Bacteriology | volume = 182 | issue = 14 | pages = 3929–33 | date = July 2000 | pmid = 10869069 | pmc = 94576 | doi = 10.1128/JB.182.14.3929-3933.2000 }} These proteins are small, basic, and dimeric nucleic acid-binding proteins. Furthermore, it is conserved in most sequenced Archaea genomes.{{cite journal | vauthors = Goyal M, Banerjee C, Nag S, Bandyopadhyay U | title = The Alba protein family: Structure and function | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1864 | issue = 5 | pages = 570–83 | date = May 2016 | pmid = 26900088 | doi = 10.1016/j.bbapap.2016.02.015 }}{{cite journal | vauthors = Wardleworth BN, Russell RJ, Bell SD, Taylor GL, White MF | title = Structure of Alba: an archaeal chromatin protein modulated by acetylation | journal = The EMBO Journal | volume = 21 | issue = 17 | pages = 4654–62 | date = September 2002 | pmid = 12198167 | pmc = 125410 | doi = 10.1093/emboj/cdf465 }} The acetylation state of Alba affects promoter access and transcription in vitro, whereas the methylation state of another Sulfolobus chromatin protein, Sso7D, is altered by culture temperature.{{cite journal | vauthors = Bell SD, Botting CH, Wardleworth BN, Jackson SP, White MF | title = The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation | journal = Science | volume = 296 | issue = 5565 | pages = 148–51 | date = April 2002 | pmid = 11935028 | doi = 10.1126/science.1070506 | bibcode = 2002Sci...296..148B | s2cid = 27858056 }}{{cite journal | vauthors = Baumann H, Knapp S, Lundbäck T, Ladenstein R, Härd T | title = Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus | journal = Nature Structural Biology | volume = 1 | issue = 11 | pages = 808–19 | date = November 1994 | pmid = 7634092 | doi = 10.1038/nsb1194-808 | s2cid = 37220619 }}

The work of Wolfram Zillig's group, which represented early evidence of the eukaryotic characteristics of transcription in Archaea has since made Sulfolobus an ideal model system for transcription studies. Recent studies in Sulfolobus in addition to other Archaea species, mainly focus on the composition, function, and regulation of the transcription machinery, and on fundamental conserved aspects of this process in both Eukaryotes and Archaea.{{cite journal | vauthors = Zillig W, Stetter KO, Janeković D | title = DNA-dependent RNA polymerase from the archaebacterium Sulfolobus acidocaldarius | journal = European Journal of Biochemistry | volume = 96 | issue = 3 | pages = 597–604 | date = June 1979 | pmid = 380989 | doi = 10.1111/j.1432-1033.1979.tb13074.x | doi-access = free }}

Exposure of Saccharolobus solfataricus to DNA damaging agents, such as ultraviolet (UV) irradiation, bleomycin, or mitomycin C, induces cellular aggregation.{{cite journal | vauthors = Fröls S, Ajon M, Wagner M, Teichmann D, Zolghadr B, Folea M, Boekema EJ, Driessen AJ, Schleper C, Albers SV | display-authors = 6 | title = UV-inducible cellular aggregation of the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by pili formation | journal = Molecular Microbiology | volume = 70 | issue = 4 | pages = 938–52 | date = November 2008 | pmid = 18990182 | doi = 10.1111/j.1365-2958.2008.06459.x | url = https://pure.rug.nl/ws/files/56956856/UV_inducible_cellular_aggregation_of_the_hyperthermophilic_archaeon_Sulfolobus_solfataricus_is_mediated_by_pili_formation.pdf | doi-access = free }} Other physical stressors like changes in pH or temperature, do not induce aggregation, suggesting that the induction of aggregation is caused specifically by DNA damage. Ajon et al.{{cite journal | vauthors = Ajon M, Fröls S, van Wolferen M, Stoecker K, Teichmann D, Driessen AJ, Grogan DW, Albers SV, Schleper C | display-authors = 6 | title = UV-inducible DNA exchange in hyperthermophilic archaea mediated by type IV pili | journal = Molecular Microbiology | volume = 82 | issue = 4 | pages = 807–17 | date = November 2011 | pmid = 21999488 | doi = 10.1111/j.1365-2958.2011.07861.x | url = https://pure.rug.nl/ws/files/6771142/2011MolMicrobiolAjon.pdf | doi-access = free }} showed that UV-induced cellular aggregation mediates chromosomal marker exchange with high frequency. Recombination rates exceeded those of uninduced cultures by up to three orders of magnitude. Frols et al.{{cite journal | vauthors = Fröls S, White MF, Schleper C | title = Reactions to UV damage in the model archaeon Sulfolobus solfataricus | journal = Biochemical Society Transactions | volume = 37 | issue = Pt 1 | pages = 36–41 | date = February 2009 | pmid = 19143598 | doi = 10.1042/BST0370036 | s2cid = 837167 }} and Ajon et al. hypothesized that the UV-induced DNA transfer process and subsequent homologous recombinational repair represents an important mechanism to maintain chromosome integrity. This response may be a primitive form of sexual interaction, similar to the more well-studied bacterial transformation that is also associated with DNA transfer between cells, leading to homologous recombinational repair of DNA damage.Bernstein H, Bernstein C (2010). "Evolutionary origin of recombination during meiosis". BioScience. 60 (7): 498–505. doi:10.1525/bio.2010.60.7.5. S2CID 86663600

Sulfolobus solfataricus is known to grow by chemoorganotrophy with the presence of oxygen while on a variety of organic compounds such as sugars, alcohols, amino acids, and aromatic compounds like phenol.{{cite journal | vauthors = Ulas T, Riemer SA, Zaparty M, Siebers B, Schomburg D | title = Genome-scale reconstruction and analysis of the metabolic network in the hyperthermophilic archaeon Sulfolobus solfataricus | journal = PLOS ONE | volume = 7 | issue = 8 | pages = e43401 | date = 2012-08-31 | pmid = 22952675 | pmc = 3432047 | doi = 10.1371/journal.pone.0043401 | bibcode = 2012PLoSO...743401U | doi-access = free }}

It uses a modified Entner-Doudroff pathway for glucose oxidation and the resulting pyruvate molecules can be totally mineralized in a TCA cycle.

Molecular oxygen is the only known electron acceptor at the end of the electron transport chain.{{cite journal | vauthors = Simon G, Walther J, Zabeti N, Combet-Blanc Y, Auria R, van der Oost J, Casalot L | title = Effect of O2 concentrations on Sulfolobus solfataricus P2 | journal = FEMS Microbiology Letters | volume = 299 | issue = 2 | pages = 255–60 | date = October 2009 | pmid = 19735462 | doi = 10.1111/j.1574-6968.2009.01759.x | doi-access = free }} Other than organic molecules, this Archaea species can also utilize hydrogen sulfide{{cite journal | vauthors = She Q, Singh RK, Confalonieri F, Zivanovic Y, Allard G, Awayez MJ, Chan-Weiher CC, Clausen IG, Curtis BA, De Moors A, Erauso G, Fletcher C, Gordon PM, Heikamp-de Jong I, Jeffries AC, Kozera CJ, Medina N, Peng X, Thi-Ngoc HP, Redder P, Schenk ME, Theriault C, Tolstrup N, Charlebois RL, Doolittle WF, Duguet M, Gaasterland T, Garrett RA, Ragan MA, Sensen CW, Van der Oost J | display-authors = 6 | title = The complete genome of the crenarchaeon Sulfolobus solfataricus P2 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 14 | pages = 7835–40 | date = July 2001 | pmid = 11427726 | pmc = 35428 | doi = 10.1073/pnas.141222098 | bibcode = 2001PNAS...98.7835S | doi-access = free }} and elementary sulfur as electron donors and fix {{CO2}}, possibly by means of the HP/HB cycle, making it also capable of living by chemoautotrophy. Recent studies have also found the capability to grow, albeit slowly, by oxidizing molecular hydrogen.

Ferredoxin is suspected to act as the major metabolic electron carrier in S. solfataricus. This contrasts with most species within the Bacteria and Eukaryote groups of organisms, which generally rely on nicotinamide adenine dinucleotide hydrogen (NADH) as the main electron carrier. S. solfataricus has strong eukaryotic features coupled with many uniquely archaeal-specific abilities. The results of the findings came from the varied methods of their DNA mechanisms, cell cycles, and transitional apparatus. Overall, the study was a prime example of the differences found in Thermoproteota and "Euryarchaeota".{{cite journal|vauthors=Zillig W, Stetter KO, Wunderl S, Schulz W, Priess H, Scholz I|date=April 1980|title=The Sulfolobus-"Caldariella" group: taxonomy on the basis of the structure of DNA-dependent RNA polymerases.|journal=Archives of Microbiology|volume=125|issue=3|pages=259–69|doi=10.1007/BF00446886|bibcode=1980ArMic.125..259Z |s2cid=5805400}}

File:Solfatara_volcano.jpg

S. solfataricus is an extreme thermophile from the Archaea family. S. solfataricus, and the members of the related genus Sulfolobus have optimal growth conditions in strong volcanic activity areas with high temperatures and very acidic pH.{{cite journal | vauthors = Grogan DW | title = Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains | journal = Journal of Bacteriology | volume = 171 | issue = 12 | pages = 6710–9 | date = December 1989 | pmid = 2512283 | pmc = 210567 | doi = 10.1128/jb.171.12.6710-6719.1989 }} These specific conditions are typical of volcanic areas such as geyser or thermal springs. In fact, the most studied countries where these microorganisms were found are the U.S.A. (Yellowstone National Park),{{cite web|url=https://microbewiki.kenyon.edu/index.php/Sulfolobus|title=Sulfolobus|website=Microbewiki}} New Zealand,{{cite journal | vauthors = Hetzer A, Morgan HW, McDonald IR, Daughney CJ | title = Microbial life in Champagne Pool, a geothermal spring in Waiotapu, New Zealand | journal = Extremophiles | volume = 11 | issue = 4 | pages = 605–14 | date = July 2007 | pmid = 17426919 | doi = 10.1007/s00792-007-0073-2 | s2cid = 24239907 }} Iceland and Italy, notorious for volcanic phenomena. A study conducted by a team of Indonesian scientists has also shown the presence of a Sulfolobus community in West Java, confirming that high temperatures, low pH, and the presence of sulfur are necessary conditions for the growth of these microbes.{{cite journal | vauthors = Aditiawati P, Yohandini H, Madayanti F | title = Microbial diversity of acidic hot spring (kawah hujan B) in geothermal field of kamojang area, west java-indonesia | journal = The Open Microbiology Journal | volume = 3 | pages = 58–66 | year = 2009 | pmid = 19440252 | pmc = 2681175 | doi = 10.2174/1874285800903010058 |doi-access=free}}

S. solfataricus is able to oxidize sulfur according to metabolic strategy. One of the products of these reactions is H+ and consequently, it will slowly acidify the surrounding area. Soil acidification increases in places where there are emissions of pollutants from industrial activity. This process reduces the number of heterotrophic bacteria involved in decomposition, which are fundamental for the process of recycling organic matter and ultimately slows the fertilization of soil.{{cite journal | vauthors = Bryant RD, Gordy EA, Laishley EJ |title=Effect of soil acidification on the soil microflora|journal=Water, Air, and Soil Pollution |volume=11 |issue=4 |pages=437 |doi=10.1007/BF00283435 |year=1979 |bibcode=1979WASP...11..437B |s2cid=96729369}}

{{clear}}

There is interest in using S. sulfataricus as a source of thermal stability enzymes for research and diagnostics as well as industries such as food, textile, cleaning, and the pulp and paper industry. Furthermore, this enzyme is overloaded due to its catalytic diversity, high pH, and temperature stability, increased to resistance organic solvents and resistance to proteolysis.{{Cite journal|last=Stepankova|first=Veronika|date=October 14, 2013|title=Strategies for Stabilization of Enzymes in Organic Solvents|journal=ACS Catalysis|volume=3|issue=12|pages=2823–2836|doi=10.1021/cs400684x}}{{Cite journal|last=DANIEL|first=R. M.|date=1982|title=A correlation between protein thermostability and resistance to proteolysis|journal= Biochemical Journal|volume=207|issue=3|pages=641–644|pmc=1153914|pmid=6819862|doi=10.1042/bj2070641}}

At present, tetra ester lipids, membrane vesicles with antimicrobial properties, trehalose components, and new β-galactooligosaccharides are becoming increasingly important.{{Cite journal|last=Quehenberger|first=Julian|date=2017|title=Sulfolobus – A Potential Key Organism in Future Biotechnology|journal= Frontiers in Microbiology|volume=8|pages=2474|doi=10.3389/fmicb.2017.02474|pmid=29312184|pmc=5733018|doi-access=free}}

{{see also|Beta-galactosidase}}

The thermostable enzyme β-galactosidase was isolated from the extreme thermophile archaebacterial S. solfataricus, strain MT-4.

This enzyme is utilized in many industrial processes of lactose containing fluids by purifying and characterizing their physicochemical properties.{{Cite journal|last=M. PISANI|first=Francesca|date=1990|title=Thermostable P-galactosidase from the archaebacterium Sulfolobus solfataricus|journal= European Journal of Biochemistry|volume=187|issue=2|pages=321–328|doi=10.1111/j.1432-1033.1990.tb15308.x|pmid=2105216|doi-access=free}}

{{see also|Protease}}

The industry are interested in stable proteases as well as in many different Sulfolobus proteases that have been studied.{{Cite book|title=Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus|journal = Biochimica et Biophysica Acta (BBA) - General Subjects|volume = 1033|issue = 2|last=Hanner|first=Markus|publisher=Elsevier B.V.|year=1990|isbn=0117536121|pages=148–153|doi = 10.1016/0304-4165(90)90005-H|pmid = 2106344}}

An active aminopeptidase associated with the chaperonin of S. solfataricus MT4 was described.{{Cite journal|last1=Condo|first1=Ivano|last2=Ruggero|first2=Davide|date=1998|title=A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol.|journal= Molecular Microbiology|volume=29|issue=3|pages=775–785|doi=10.1046/j.1365-2958.1998.00971.x|pmid=9723917|doi-access=free}}

Sommaruga et al. (2014){{Cite journal|last=Sommaruga|first=Silvia|date=2014|title=mmobilization of carboxypeptidase from Sulfolobus solfataricus on magnetic nanoparticles improves enzyme stability and functionality in organic media. BMC Biotechnol.|journal= BMC Biotechnology|volume=14|issue=1|pages=82|doi=10.1186/1472-6750-14-82|pmid=25193105|pmc=4177664 |doi-access=free }} also improved the stability and reaction yield of a well-characterized carboxypeptidase from S. solfataricus MT4 by magnetic nanoparticles immobilizing the enzyme.

{{see also|Lipase}}

A new thermostable extracellular lipolytic enzyme serine arylesterase was originally discovered for their large action in the hydrolysis of organophosphates from the thermoacidophilic archaeon S. solfataricus P1.{{Cite journal|last=Park|first=Young-Jun|date=2016|title= Purification and characterization of a new inducible thermostable extracellular lipolytic enzyme from the thermoacidophilic archaeon Sulfolobus solfataricus P1|journal= Journal of Molecular Catalysis B: Enzymatic|volume=124|pages=11–19|doi=10.1016/j.molcatb.2015.11.023}}

{{see also|Chaperonin ATPase}}

In reaction to temperature shock (50.4 °C) in E. coli cells, a tiny warm stun protein (S.so-HSP20) from S.solfataricus P2 has been effectively used to improve tolerance to temperature.{{Cite journal|last=Li|first=Dong-Chol|date=August 2011|title=Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2. Cell Stress Chaperones|journal= Cell Stress & Chaperones|volume=17|issue=1|pages=103–108|doi=10.1007/s12192-011-0289-z|pmid=21853411|pmc=3227843}}

Since chaperonin Ssocpn (920 kDa), which includes adenosine triphosphate (ATP), K+, and Mg² +, has not produced any additional proteins in S. solfataricus to supply collapsed and dynamic proteins from denatured materials, it was stored on an ultrafiltration cell, while the renatured substrates were moving through the film.{{Cite journal|last=Cerchia|first=Laura|date=7 August 1999|title=An archaeal chaperonin-based reactor for renaturation of denatured proteins. Extremophile|journal= Extremophiles: Life Under Extreme Conditions|volume=4|issue=1|pages=1–7|doi=10.1007/s007920050001|pmid=10741831|s2cid=25407893}}

{{see also|Liposome}}

Because of its tetraether lipid material, the membrane of extreme thermophilic Archaea is unique in its composition. Archaea lipids are a promising source of liposomes with exceptional stability of temperature, pH, and tightness against the leakage of solute. Such archaeosomes are possible instruments for the delivery of medicines, vaccines, and genes.{{Cite journal|last=B. Patel|first=Girishchandra|date=1999|title=Archaeobacterial Ether Lipid Liposomes (Archaeosomes) as Novel Vaccine and Drug Delivery Systems|journal=Critical Reviews in Biotechnology|volume=19|issue=4|pages=317–357|doi=10.1080/0738-859991229170|pmid=10723627}}

• List of Archaea genera

{{Reflist|32em}}

{{refbegin|32em}}

• {{cite journal | vauthors = Fiorentino G, Del Giudice I, Petraccone L, Bartolucci S, Del Vecchio P | title = Conformational stability and ligand binding properties of BldR, a member of the MarR family, from Sulfolobus solfataricus | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1844 | issue = 6 | pages = 1167–72 | date = June 2014 | pmid = 24704039 | doi = 10.1016/j.bbapap.2014.03.011 }}
• {{cite journal | vauthors = de Rosa M, Bemporad F, Pellegrino S, Chiti F, Bolognesi M, Ricagno S | title = Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase | journal = The FEBS Journal | volume = 281 | issue = 18 | pages = 4072–84 | date = September 2014 | pmid = 24893801 | doi = 10.1111/febs.12861 | doi-access = free }}
• {{cite journal | vauthors = Gamsjaeger R, Kariawasam R, Touma C, Kwan AH, White MF, Cubeddu L | title = Backbone and side-chain ¹H, ¹³C and ¹⁵N resonance assignments of the OB domain of the single stranded DNA binding protein from Sulfolobus solfataricus and chemical shift mapping of the DNA-binding interface | journal = Biomolecular NMR Assignments | volume = 8 | issue = 2 | pages = 243–6 | date = October 2014 | pmid = 23749431 | doi = 10.1007/s12104-013-9492-4 | s2cid = 6388231 }}
• {{cite journal | vauthors = Wang J, Zhu J, Min C, Wu S | title = CBD binding domain fused γ-lactamase from Sulfolobus solfataricus is an efficient catalyst for (-) γ-lactam production | journal = BMC Biotechnology | volume = 14 | pages = 40 | date = May 2014 | pmid = 24884655 | pmc = 4041915 | doi = 10.1186/1472-6750-14-40 | doi-access = free }}

{{refend}}

• [http://bacdive.dsmz.de/index.php?search=16650&submit=Search Type strain of Sulfolobus solfataricus at BacDive - the Bacterial Diversity Metadatabase]

{{Archaea classification}}

{{Taxonbar|from=Q3503466}}

Category:Thermoproteota

Category:Archaea described in 1980