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=== Structure and assembly: type IV pilus and archaellum ===
=== Structure and assembly: type IV pilus and archaellum ===


In the 1980s, Dieter Oesterhelt’s laboratory showed for the first time that [[haloarchaea]] switch the rotation of their archaellum from clockwise to counterclockwise upon blue light pulses.<ref>Alam, M. & Oesterhelt, D. Morphology, function and isolation of halobacterial flagella. J Mol Biol 176, 459-75 (1984).</ref><ref> Marwan, W., Alam, M. & Oesterhelt, D. Rotation and switching of the flagellar motor assembly in Halobacterium halobium. J Bacteriol 173, 1971-7 (1991).</ref> This led microbiologists to believe that the archaeal motility structure is not only functionally, but also structurally reminiscent of bacterial flagella. However, in contrast to [[flagellin]]s, archaellins are produced as preproteins which are processed by a specific peptidase prior to assembly. Their signal peptide is homologous to class III signal peptides of type IV prepilins that are processed in Gram-negative bacteria by the peptidase PilD.<ref>Faguy, D.M., Jarrell, K.F., Kuzio, J. & Kalmokoff, M.L. Molecular analysis of archael flagellins: similarity to the type IV pilin-transport superfamily widespread in bacteria. Can J Microbiol 40, 67-71 (1994).</ref> In crenarchaeota PibD and in euryarchaeota FlaK are PilD homologs, that are essential for the maturation of the archaellins. Furthermore, archaellins are N-glycosylated<ref>Jarrell, K.F., Jones, G.M., Kandiba, L., Nair, D.B. & Eichler, J. S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications. Archaea 2010 (2010).</ref><ref>Meyer, B.H., Zolghadr, B., Peyfoon, E., Pabst, M., Panico, M., Morris, H.R., Haslam, S.M., Messner, P., Schaffer, C., Dell, A. & Albers, S. Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius. Mol Microbiol 82, 1150-1163 (2011).</ref> which has not been described for bacterial flagellins, where O-linked glycosylation is evident. Two other components of the archaellum assembly system, namely, FlaI and FlaJ are homologous to components of type IV pili, PilB and PilC, respectively. Moreover, the structure of the archaellum filament resembles archaeal and bacterial type IV pili as it has no central lumen<ref>Trachtenberg, S., Galkin, V.E. & Egelman, E.H. Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: insights into polymorphism. J Mol Biol 346, 665-76 (2005).</ref><ref name=Wang>{{cite journal | vauthors = Wang F, Cvirkaite-Krupovic V, Kreutzberger MA, Su Z, de Oliveira GA, Osinski T, Sherman N, DiMaio F, Wall JS, Prangishvili D, Krupovic M, Egelman EH | title = An extensively glycosylated archaeal pilus survives extreme conditions | journal = Nature Microbiology | date = May 2019 | pmid = 31110358 | doi = 10.1038/s41564-019-0458-x }}</ref> excluding the possibility that it might assembled in a similar fashion like bacterial flagella via a type III secretion system.<ref>Macnab, R.M. Genetics and biogenesis of bacterial flagella. Annu Rev Genet 26, 131-58 (1992).</ref> Additionally, it was demonstrated that the rotation of the archaellum is dependent on ATP concentration in the cell rather than PMF ([[Electrochemical gradient|proton motive force]]) as in the bacterial flagellum.<ref>Streif, S., Staudinger, W.F., Marwan, W. & Oesterhelt, D. Flagellar rotation in the archaeon Halobacterium salinarum depends on ATP. Journal of Molecular Biology 384, 1-8 (2008).</ref>
In the 1980s, Dieter Oesterhelt’s laboratory showed for the first time that [[haloarchaea]] switch the rotation of their archaellum from clockwise to counterclockwise upon blue light pulses.<ref name="pmid6748081">{{cite journal | vauthors = Alam M, Oesterhelt D | title = Morphology, function and isolation of halobacterial flagella | journal = Journal of Molecular Biology | volume = 176 | issue = 4 | pages = 459–75 | date = July 1984 | pmid = 6748081 | doi = | url = }}</ref><ref name="pmid2002000">{{cite journal | vauthors = Marwan W, Alam M, Oesterhelt D | title = Rotation and switching of the flagellar motor assembly in Halobacterium halobium | journal = Journal of Bacteriology | volume = 173 | issue = 6 | pages = 1971–7 | date = March 1991 | pmid = 2002000 | doi = 10.1128/jb.173.6.1971-1977.1991 }}</ref> This led microbiologists to believe that the archaeal motility structure is not only functionally, but also structurally reminiscent of bacterial flagella. However, in contrast to [[flagellin]]s, archaellins are produced as preproteins which are processed by a specific peptidase prior to assembly. Their signal peptide is homologous to class III signal peptides of type IV prepilins that are processed in Gram-negative bacteria by the peptidase PilD.<ref name="pmid7908603">{{cite journal | vauthors = Faguy DM, Jarrell KF, Kuzio J, Kalmokoff ML | title = Molecular analysis of archael flagellins: similarity to the type IV pilin-transport superfamily widespread in bacteria | journal = Canadian Journal of Microbiology | volume = 40 | issue = 1 | pages = 67–71 | date = January 1994 | pmid = 7908603 | doi = | url = }}</ref> In crenarchaeota PibD and in euryarchaeota FlaK are PilD homologs, that are essential for the maturation of the archaellins. Furthermore, archaellins are N-glycosylated<ref name="pmid20721273">{{cite journal | vauthors = Jarrell KF, Jones GM, Kandiba L, Nair DB, Eichler J | title = S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications | journal = Archaea (Vancouver, B.C.) | volume = 2010 | issue = | pages = | date = July 2010 | pmid = 20721273 | pmc = 2913515 | doi = 10.1155/2010/612948 }}</ref><ref name="pmid22059775">{{cite journal | vauthors = Meyer BH, Zolghadr B, Peyfoon E, Pabst M, Panico M, Morris HR, Haslam SM, Messner P, Schäffer C, Dell A, Albers SV | title = Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius | journal = Molecular Microbiology | volume = 82 | issue = 5 | pages = 1150–63 | date = December 2011 | pmid = 22059775 | pmc = 4391026 | doi = 10.1111/j.1365-2958.2011.07875.x }}</ref> which has not been described for bacterial flagellins, where O-linked glycosylation is evident. Two other components of the archaellum assembly system, namely, FlaI and FlaJ are homologous to components of type IV pili, PilB and PilC, respectively. Moreover, the structure of the archaellum filament resembles archaeal and bacterial type IV pili as it has no central lumen<ref name="pmid15713454">{{cite journal | vauthors = Trachtenberg S, Galkin VE, Egelman EH | title = Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: insights into polymorphism | journal = Journal of Molecular Biology | volume = 346 | issue = 3 | pages = 665–76 | date = February 2005 | pmid = 15713454 | doi = 10.1016/j.jmb.2004.12.010 }}</ref><ref name=Wang>{{cite journal | vauthors = Wang F, Cvirkaite-Krupovic V, Kreutzberger MA, Su Z, de Oliveira GA, Osinski T, Sherman N, DiMaio F, Wall JS, Prangishvili D, Krupovic M, Egelman EH | title = An extensively glycosylated archaeal pilus survives extreme conditions | journal = Nature Microbiology | date = May 2019 | pmid = 31110358 | doi = 10.1038/s41564-019-0458-x }}</ref> excluding the possibility that it might assembled in a similar fashion like bacterial flagella via a type III secretion system.<ref name="pmid1482109">{{cite journal | vauthors = Macnab RM | title = Genetics and biogenesis of bacterial flagella | journal = Annual Review of Genetics | volume = 26 | issue = | pages = 131–58 | date = 1992 | pmid = 1482109 | doi = 10.1146/annurev.ge.26.120192.001023 }}</ref> Additionally, it was demonstrated that the rotation of the archaellum is dependent on ATP concentration in the cell rather than PMF ([[Electrochemical gradient|proton motive force]]) as in the bacterial flagellum.<ref name="pmid18786541">{{cite journal | vauthors = Streif S, Staudinger WF, Marwan W, Oesterhelt D | title = Flagellar rotation in the archaeon Halobacterium salinarum depends on ATP | journal = Journal of Molecular Biology | volume = 384 | issue = 1 | pages = 1–8 | date = December 2008 | pmid = 18786541 | doi = 10.1016/j.jmb.2008.08.057 }}</ref>
<!-- Deleted image removed: [[File:Model-archaellum.gif|thumb|'''Model of the crenarchaeal and euryarchaeal flagella assembly systems.''' FlaJ and FlaI form the membrane platform of the flagellum structure. After processing by FlaK/PibD, the flagellins are assembled into the flagellum. In Crenarchaeota, the accessory proteins are all localized in the membrane, except for FlaH, which might be involved in the modulation of FlaI activity. Euryarchaeal FlaC/D/E are involved in transducing intra/extra-cellular signals that influence the activity of the flagellum.
<!-- Deleted image removed: [[File:Model-archaellum.gif|thumb|'''Model of the crenarchaeal and euryarchaeal flagella assembly systems.''' FlaJ and FlaI form the membrane platform of the flagellum structure. After processing by FlaK/PibD, the flagellins are assembled into the flagellum. In Crenarchaeota, the accessory proteins are all localized in the membrane, except for FlaH, which might be involved in the modulation of FlaI activity. Euryarchaeal FlaC/D/E are involved in transducing intra/extra-cellular signals that influence the activity of the flagellum.<ref name="pmid21265748">{{cite journal | vauthors = Ghosh A, Albers SV | title = Assembly and function of the archaeal flagellum | journal = Biochemical Society Transactions | volume = 39 | issue = 1 | pages = 64–9 | date = January 2011 | pmid = 21265748 | doi = 10.1042/BST0390064 }}</ref>]] -->

This figure was originally published in Biochemical Society Transactions: Abhrajyoti Ghosh and Sonja Verena Albers, Assembly and function of the archaeal flagellum, in Biochemical Society Transactions 2011, 39, (64–69) doi:10.1042/BST0390064 © Biochemical Society]] -->


=== Functional analogs ===
=== Functional analogs ===


Despite the limited number of details presently available regarding the structure and assembly of archaellum, it has become increasingly evident from multiple studies that archaella play important roles in a variety of cellular processes in archaea. In spite of the structural dissimilarities with the bacterial flagellum, the main function thus far attributed for archaellum is swimming in liquid<ref name="Lassak_2012" /><ref>Alam, M., Claviez, M., Oesterhelt, D. & Kessel, M. Flagella and motility behaviour of square bacteria. EMBO J 3, 2899-903 (1984).</ref><ref>Herzog, B. & Wirth, R. Swimming behavior of selected species of Archaea. Appl Environ Microbiol 78, 1670-4 (2012).</ref> and semi-solid surfaces.<ref>Szabó, Z., Sani, M., Groeneveld, M., Zolghadr, B., Schelert, J., Albers, S.-V., Blum, P., Boekema, E. & Driessen, A. Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus. Journal of Bacteriology 189, 4305-4309 (2007).</ref><ref>Jarrell, K.F., Bayley, D.P., Florian, V. & Klein, A. Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae. Mol Microbiol 20, 657-66 (1996).</ref> Increasing biochemical and biophysical information has further consolidated the early observations of archaella mediated swimming in archaea. Like the bacterial flagellum,<ref>Henrichsen, J. Bacterial surface translocation: a survey and a classification. Bacteriol Rev 36, 478-503 (1972).</ref><ref>Jarrell, K.F. & McBride, M.J. The surprisingly diverse ways that prokaryotes move. Nat Rev Microbiol 6, 466-76 (2008).</ref> the archaellum also mediates surface attachment and cell-cell communication.<ref>Näther, D.J., Rachel, R., Wanner, G. & Wirth, R. Flagella of Pyrococcus furiosus: multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts. Journal of Bacteriology 188, 6915-6923 (2006).</ref><ref>Zolghadr, B., Klingl, A., Koerdt, A., Driessen, A.J., Rachel, R. & Albers, S.V. Appendage-mediated surface adherence of Sulfolobus solfataricus. J Bacteriol 192, 104-10 (2010).</ref> However, unlike the bacterial flagellum archaellum has not shown to play a role in archaeal biofilm formation.<ref>Koerdt, A., Godeke, J., Berger, J., Thormann, K.M. & Albers, S.V. Crenarchaeal biofilm formation under extreme conditions. PLoS One 5, e14104 (2010).</ref> In archaeal biofilms, the only proposed function is thus far during the dispersal phase of biofilm when archaeal cells escape the community using their archaellum to further initiate the next round of biofilm formation. Also, archaellum have been found to be able to have a metal-binding site .<ref>Meshcheryakov, Vladimir A, et al. “High‐Resolution Archaellum Structure Reveals a Conserved Metal‐Binding Site.” EMBO Reports, 2019, doi:10.15252/embr.201846340.</ref>
Despite the limited number of details presently available regarding the structure and assembly of archaellum, it has become increasingly evident from multiple studies that archaella play important roles in a variety of cellular processes in archaea. In spite of the structural dissimilarities with the bacterial flagellum, the main function thus far attributed for archaellum is swimming in liquid<ref name="Lassak_2012" /><ref name="pmid6526006">{{cite journal | vauthors = Alam M, Claviez M, Oesterhelt D, Kessel M | title = Flagella and motility behaviour of square bacteria | journal = The EMBO Journal | volume = 3 | issue = 12 | pages = 2899–903 | date = December 1984 | pmid = 6526006 | doi = | url = }}</ref<ref name="pmid22247169">{{cite journal | vauthors = Herzog B, Wirth R | title = Swimming behavior of selected species of Archaea | journal = Applied and Environmental Microbiology | volume = 78 | issue = 6 | pages = 1670–4 | date = March 2012 | pmid = 22247169 | pmc = 3298134 | doi = 10.1128/AEM.06723-11 }}</ref> and semi-solid surfaces.<ref name="pmid17416662">{{cite journal | vauthors = Szabó Z, Sani M, Groeneveld M, Zolghadr B, Schelert J, Albers SV, Blum P, Boekema EJ, Driessen AJ | title = Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus | journal = Journal of Bacteriology | volume = 189 | issue = 11 | pages = 4305–9 | date = June 2007 | pmid = 17416662 | pmc = 1913377 | doi = 10.1128/JB.00042-07 }}</ref><ref name="pmid8736544">{{cite journal | vauthors = Jarrell KF, Bayley DP, Florian V, Klein A | title = Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae | journal = Molecular Microbiology | volume = 20 | issue = 3 | pages = 657–66 | date = May 1996 | pmid = 8736544 | doi = | url = }}</ref> Increasing biochemical and biophysical information has further consolidated the early observations of archaella mediated swimming in archaea. Like the bacterial flagellum,<ref name="pmid4631369">{{cite journal | vauthors = Henrichsen J | title = Bacterial surface translocation: a survey and a classification | journal = Bacteriological Reviews | volume = 36 | issue = 4 | pages = 478–503 | date = December 1972 | pmid = 4631369 | pmc = 408329 | doi = | url = }}</ref><ref name="pmid18461074">{{cite journal | vauthors = Jarrell KF, McBride MJ | title = The surprisingly diverse ways that prokaryotes move | journal = Nature Reviews. Microbiology | volume = 6 | issue = 6 | pages = 466–76 | date = June 2008 | pmid = 18461074 | doi = 10.1038/nrmicro1900 }}</ref> the archaellum also mediates surface attachment and cell-cell communication.<ref name="pmid16980494">{{cite journal | vauthors = Näther DJ, Rachel R, Wanner G, Wirth R | title = Flagella of Pyrococcus furiosus: multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts | journal = Journal of Bacteriology | volume = 188 | issue = 19 | pages = 6915–23 | date = October 2006 | pmid = 16980494 | pmc = 1595509 | doi = 10.1128/JB.00527-06 }}</ref><ref name="pmid19854908">{{cite journal | vauthors = Zolghadr B, Klingl A, Koerdt A, Driessen AJ, Rachel R, Albers SV | title = Appendage-mediated surface adherence of Sulfolobus solfataricus | journal = Journal of Bacteriology | volume = 192 | issue = 1 | pages = 104–10 | date = January 2010 | pmid = 19854908 | pmc = 2798249 | doi = 10.1128/JB.01061-09 }}</ref> However, unlike the bacterial flagellum archaellum has not shown to play a role in archaeal biofilm formation.<ref name="pmid21124788">{{cite journal | vauthors = Koerdt A, Gödeke J, Berger J, Thormann KM, Albers SV | title = Crenarchaeal biofilm formation under extreme conditions | journal = Plos One | volume = 5 | issue = 11 | pages = e14104 | date = November 2010 | pmid = 21124788 | pmc = 2991349 | doi = 10.1371/journal.pone.0014104 }}</ref> In archaeal biofilms, the only proposed function is thus far during the dispersal phase of biofilm when archaeal cells escape the community using their archaellum to further initiate the next round of biofilm formation. Also, archaellum have been found to be able to have a metal-binding site.<ref name="pmid30898768">{{cite journal | vauthors = Meshcheryakov VA, Shibata S, Schreiber MT, Villar-Briones A, Jarrell KF, Aizawa SI, Wolf M | title = High-resolution archaellum structure reveals a conserved metal-binding site | journal = EMBO Reports | volume = 20 | issue = 5 | pages = | date = May 2019 | pmid = 30898768 | pmc = 6500986 | doi = 10.15252/embr.201846340 }}</ref>


== References ==
== References ==

Revision as of 07:35, 25 May 2019

An archaellum (plural: archaella, formerly archaeal flagellum) is a unique whip-like structure on the cell surface of many archaea. The name was proposed in 2012 following studies that showed it to be evolutionarily and structurally different from the bacterial and eukaryotic flagella. The archaellum is functionally the same – it can be rotated and is used to swim in liquid environments. The archaellum was found to be structurally similar to the type IV pilus.[1][2]

History

In 1977, archaea were first classified as a separate group of prokaryotes in the three-domain system of Carl Woese and George E. Fox, based on the differences in the sequence of ribosomal RNA (16S rRNA) genes.[3][4] This domain possesses numerous fundamental traits distinct from both the bacterial and the eukaryotic domains. Many archaea possess a rotating motility structure that at first seemed to resemble the bacterial and eukaryotic flagella. The flagellum (Latin for whip) is a lash-like appendage that protrudes from the cell. In the last two decades, it was discovered that the archaeal flagella, although functionally similar to bacterial and eukaryotic flagella, structurally resemble bacterial type IV pili.[5][6][7] Bacterial type IV pili are surface structures that can be extended and retracted to give a twitching motility and are used to adhere to or move on solid surfaces; their "tail" proteins are called pilins.[8][9] To underline these differences, Ken Jarrell and Sonja-Verena Albers proposed to change the name of the archaeal flagellum to archaellum.[10]

Structure

Electron micrographs of Sulfolobus acidocaldarius MW001 during normal growth. Indication of archaella (black arrows) and pili (white arrows). Negative staining with uranyl acetate.

Components

2015 model of the crenarchaeal archaellum.[1] By 2018, flaH is known to be present in five copies.[11]

Most proteins that make up the archaellum are encoded within one genetic locus. This genetic locus contains 7-13 genes which encode proteins involved in either assembly or function of the archaellum.[7] The genetic locus contains genes encoding archaellins (flaA and flaB)[a] - the structural components of the filament - and motor components (flaI, flaJ, flaH). The locus furthermore encodes accessory proteins (FlaG, FlaF, FlaX) and signaling components (FlaC, FlaD, FlaE). Genetic analysis in different archaea revealed that each of these components is essential for assembly of the archaellum.[12][13][14][15][16] Whereas most of the fla-associated genes are generally found in Euryarchaeota, one or more of these genes are absent from the fla-operon in Crenarchaeota. The prepilin peptidase (called PibD in crenarchaeota and FlaK in euryarchaeota) is essential for the maturation of the archaellins and is generally encoded elsewhere on the chromosome.[17]

Functional characterization has only been performed for FlaI, a Type II/IV secretion system ATPase super-family member[18] and PibD/FlaK.[17][19][20] FlaI forms a hexamer which hydrolyses ATP and most likely generates energy to assemble the archaellum. PibD cleaves the N-terminus of the archaellins before they can be assembled. FlaH (PDB: 2DR3​) has a RecA-like fold and inactive ATPase domains. FlaH and FlaJ are the two other core components that together with FlaI to form a core platform/motor. FlaX acts as a scaffold around the motor in Crenarchaeota.[11] The exact role of accessory proteins FlaF and FlaG is poorly understood. The genes coding for the signaling components such as flaC, flaD, flaE are only present in Euryarchaeota and interact with Chemotaxis proteins (e.g., CheY, CheD and CheC2) to sense environmental signals (such as exposure to light of specific wavelength, nutrient conditions etc.).[21]

Structure and assembly: type IV pilus and archaellum

In the 1980s, Dieter Oesterhelt’s laboratory showed for the first time that haloarchaea switch the rotation of their archaellum from clockwise to counterclockwise upon blue light pulses.[22][23] This led microbiologists to believe that the archaeal motility structure is not only functionally, but also structurally reminiscent of bacterial flagella. However, in contrast to flagellins, archaellins are produced as preproteins which are processed by a specific peptidase prior to assembly. Their signal peptide is homologous to class III signal peptides of type IV prepilins that are processed in Gram-negative bacteria by the peptidase PilD.[24] In crenarchaeota PibD and in euryarchaeota FlaK are PilD homologs, that are essential for the maturation of the archaellins. Furthermore, archaellins are N-glycosylated[25][26] which has not been described for bacterial flagellins, where O-linked glycosylation is evident. Two other components of the archaellum assembly system, namely, FlaI and FlaJ are homologous to components of type IV pili, PilB and PilC, respectively. Moreover, the structure of the archaellum filament resembles archaeal and bacterial type IV pili as it has no central lumen[27][2] excluding the possibility that it might assembled in a similar fashion like bacterial flagella via a type III secretion system.[28] Additionally, it was demonstrated that the rotation of the archaellum is dependent on ATP concentration in the cell rather than PMF (proton motive force) as in the bacterial flagellum.[29]

Functional analogs

Despite the limited number of details presently available regarding the structure and assembly of archaellum, it has become increasingly evident from multiple studies that archaella play important roles in a variety of cellular processes in archaea. In spite of the structural dissimilarities with the bacterial flagellum, the main function thus far attributed for archaellum is swimming in liquid[16]Cite error: A <ref> tag is missing the closing </ref> (see the help page). and semi-solid surfaces.[30][31] Increasing biochemical and biophysical information has further consolidated the early observations of archaella mediated swimming in archaea. Like the bacterial flagellum,[32][33] the archaellum also mediates surface attachment and cell-cell communication.[34][35] However, unlike the bacterial flagellum archaellum has not shown to play a role in archaeal biofilm formation.[36] In archaeal biofilms, the only proposed function is thus far during the dispersal phase of biofilm when archaeal cells escape the community using their archaellum to further initiate the next round of biofilm formation. Also, archaellum have been found to be able to have a metal-binding site.[37]

References

  1. ^ In some species, the names are given as FlgA and FlgB.
  1. ^ a b Albers SV, Jarrell KF (27 January 2015). "The archaellum: how Archaea swim". Frontiers in Microbiology. 6: 23. doi:10.3389/fmicb.2015.00023. PMC 4307647. PMID 25699024.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  2. ^ a b Wang F, Cvirkaite-Krupovic V, Kreutzberger MA, Su Z, de Oliveira GA, Osinski T, Sherman N, DiMaio F, Wall JS, Prangishvili D, Krupovic M, Egelman EH (May 2019). "An extensively glycosylated archaeal pilus survives extreme conditions". Nature Microbiology. doi:10.1038/s41564-019-0458-x. PMID 31110358.
  3. ^ Woese CR, Fox GE (November 1977). "Phylogenetic structure of the prokaryotic domain: the primary kingdoms". Proceedings of the National Academy of Sciences of the United States of America. 74 (11): 5088–90. doi:10.1073/pnas.74.11.5088. PMC 432104. PMID 270744.
  4. ^ Woese CR, Kandler O, Wheelis ML (June 1990). "Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya". Proceedings of the National Academy of Sciences of the United States of America. 87 (12): 4576–9. doi:10.1073/pnas.87.12.4576. PMC 54159. PMID 2112744.
  5. ^ Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, Saier MH (November 2003). "Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella". Microbiology (Reading, England). 149 (Pt 11): 3051–72. doi:10.1099/mic.0.26364-0. PMID 14600218.
  6. ^ Pohlschroder M, Ghosh A, Tripepi M, Albers SV (June 2011). "Archaeal type IV pilus-like structures--evolutionarily conserved prokaryotic surface organelles". Current Opinion in Microbiology. 14 (3): 357–63. doi:10.1016/j.mib.2011.03.002. PMID 21482178.
  7. ^ a b Ghosh A, Albers SV (January 2011). "Assembly and function of the archaeal flagellum". Biochemical Society Transactions. 39 (1): 64–9. doi:10.1042/BST0390064. PMID 21265748.
  8. ^ Craig L, Pique ME, Tainer JA (May 2004). "Type IV pilus structure and bacterial pathogenicity". Nature Reviews. Microbiology. 2 (5): 363–78. doi:10.1038/nrmicro885. PMID 15100690.
  9. ^ Craig L, Li J (April 2008). "Type IV pili: paradoxes in form and function". Current Opinion in Structural Biology. 18 (2): 267–77. doi:10.1016/j.sbi.2007.12.009. PMC 2442734. PMID 18249533.
  10. ^ Jarrell KF, Albers SV (July 2012). "The archaellum: an old motility structure with a new name". Trends in Microbiology. 20 (7): 307–12. doi:10.1016/j.tim.2012.04.007. PMID 22613456.
  11. ^ a b Albers SV, Jarrell KF (April 2018). "The Archaellum: An Update on the Unique Archaeal Motility Structure". Trends in Microbiology. 26 (4): 351–362. doi:10.1016/j.tim.2018.01.004. PMID 29452953.
  12. ^ Patenge N, Berendes A, Engelhardt H, Schuster SC, Oesterhelt D (August 2001). "The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum". Molecular Microbiology. 41 (3): 653–63. PMID 11532133.
  13. ^ Thomas NA, Bardy SL, Jarrell KF (April 2001). "The archaeal flagellum: a different kind of prokaryotic motility structure". FEMS Microbiology Reviews. 25 (2): 147–74. doi:10.1111/j.1574-6976.2001.tb00575.x. PMID 11250034.
  14. ^ Thomas NA, Mueller S, Klein A, Jarrell KF (November 2002). "Mutants in flaI and flaJ of the archaeon Methanococcus voltae are deficient in flagellum assembly". Molecular Microbiology. 46 (3): 879–87. PMID 12410843.
  15. ^ Chaban B, Ng SY, Kanbe M, Saltzman I, Nimmo G, Aizawa S, Jarrell KF (November 2007). "Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon, Methanococcus maripaludis". Molecular Microbiology. 66 (3): 596–609. doi:10.1111/j.1365-2958.2007.05913.x. PMID 17887963.
  16. ^ a b Lassak K, Neiner T, Ghosh A, Klingl A, Wirth R, Albers SV (January 2012). "Molecular analysis of the crenarchaeal flagellum". Molecular Microbiology. 83 (1): 110–24. doi:10.1111/j.1365-2958.2011.07916.x. PMID 22081969.
  17. ^ a b Bardy SL, Jarrell KF (November 2003). "Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae". Molecular Microbiology. 50 (4): 1339–47. PMID 14622420.
  18. ^ Ghosh A, Hartung S, van der Does C, Tainer JA, Albers SV (July 2011). "Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding". The Biochemical Journal. 437 (1): 43–52. doi:10.1042/BJ20110410. PMC 3213642. PMID 21506936.
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