Abstract
Actin represents one of the most abundant and conserved eukaryotic proteins over time, and has an important role in many different cellular processes such as cell shape determination, motility, force generation, cytokinesis, amongst many others. Eukaryotic actin has been studied for decades and was for a long time considered a eukaryote-specific trait. However, in the early 2000s a bacterial actin homolog, MreB, was identified, characterized and found to have a cytoskeletal function and group within the superfamily of actin proteins. More recently, an actin cytoskeleton was also identified in archaea. The genome of the hyperthermophilic crenarchaeon Pyrobaculum calidifontis contains a five-gene cluster named Arcade encoding for an actin homolog, Crenactin, polymerizing into helical filaments spanning the whole length of the cell. Phylogenetic and structural studies place Crenactin closer to the eukaryotic actin than to the bacterial homologues. A significant difference, however, is that Crenactin can form single helical filaments in addition to filaments containing two intertwined proto filaments. The genome of the recently discovered Lokiarchaeota encodes several different actin homologues, termed Lokiactins, which are even more closely related to the eukaryotic actin than Crenactin. A primitive, dynamic actin-based cytoskeleton in archaea could have enabled the engulfment of the alphaproteobacterial progenitor of the mitochondria, a key-event in the evolution of eukaryotes.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Amo T, Paje MLF, Inagaki A et al (2002) Pyrobaculum calidifontis sp. nov., a novel hyperthermophilic archaeon that grows in atmospheric air. Archaea 1:113–121
Bean GJ, Flickinger ST, Westler WM et al (2009) A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB. Biochemistry 48:4852–4857
Bernander R, Lind AE, Ettema TJG (2011) An archaeal origin for the actin cytoskeleton. Commun Integr Biol 4:664–667
Braun T, Orlova A, Valegård K et al (2015) Archaeal actin from a hyperthermophile forms a single-stranded filament. Proc Natl Acad Sci U S A 112:9340–9345
Carlier MF et al (2015) Control of polarized assembly of actin filaments in cell motility. Cell Mol Life Sci 72:3051–3067
Cooper JA (1987) Effects of cytochalasin and phalloidin on actin. J Cell Biol 105:1473–1478
Davidson AJ, Wood W (2016) Unravelling the actin cytoskeleton: a new competitive edge. Trends Cell Biol 26(8):569–576
Egelman EH, Francis N, DeRosier DJ (1982) F-actin is a helix with a random variable twist. Nature 298:131–135
Elkins JG, Podar M, Graham DE et al (2008) A korarchaeal genome reveals insights into the evolution of the Archaea. Proc Natl Acad Sci U S A 105:8102–8107
Erickson HP (2007) Evolution of the cytoskeleton. Bioessays 29:668–677
Ettema TJG, Lindås AC, Bernander R (2011) An actin-based cytoskeleton in archaea. Mol Microbiol 80:1052–1061
Eun YJ, Kapoor M, Hussain S et al (2015) Bacterial filament systems: toward understanding their emergent behaviour and cellular functions. J Biol Chem 290:17181–17189
Frixione E (2000) Recurring views on the structure and function of the cytoskeleton: a 300-year epic. Cell Motil Cytoskeleton 46:73–94
Fujii T, Iwane AH, Yanagida T et al (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467:724–728
Goodson HV, Hawse WF (2002) Molecular evolution of the actin family. J Cell Sci 115:2619–2622
Guy L, Ettema TJG (2011) The archaeal ‘TACK’ superphylum and the origin of eukaryotes. Trends Microbiol 19:580–587
Hara F, Yamashiro K, Nemoto N et al (2007) An actin homolog of the archaeon Thermoplasma acidophilum that retains the ancient characteristics of eukaryotic actin. J Bacteriol 189:2039–2045
Hennessey ES, Drummond DR, Sparrow JC (1993) Molecular genetics of actin function. Biochem J 291:657–671
Holm L, Rosenström P (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38:545–549
Holmes KC, Popp D, Gebhard W et al (1990) Atomic model of the actin filament. Nature 347:44–49
Izoré T, Duman R, Kureisaite-Ciziene D et al (2014) Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments. FEBS Lett 588:776–782
Jones LJF, Carballido-López R, Errington J (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104:913–922
Kabsch W, Mannherz HG, Suck D et al (1990) Atomic structure of the actin:DNase I complex. Nature 347:37–44
Köster DV, Mayor S (2016) Cortical actin and the plasma membrane: inextricably intertwined. Curr Opin Cell Biol 38:81–89
Lindås AC, Karlsson EA, Lindgren MT et al (2008) A unique cell division machinery in the Archaea. Proc Natl Acad Sci U S A 105:18942–18946
Lindås AC, Chruszcz M, Bernander R et al (2014) Structure of crenactin, an archaeal actin homologue active at 90 °C. Acta Crystallogr D Biol Crystallogr D70:492–500
Makarova KS, Yutin N, Bell SD et al (2010) Evolution of diverse cell division and vesicle formation systems in Archaea. Nat Rev Microbiol 8:731–741
Mishra M, Huang J, Balasubramanian MK (2014) The yeast actin cytoskeleton. FEMS Microbiol Rev 38:213–227
Pollard TD, Cooper JA (1986) Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem 55:987–1035
Pollard TD, Cooper JA (2009) Actin, a central player in cell shape and movement. Science 326:1208–1212
Roeben A, Kofler C, Nagy I et al (2006) Crystal structure of an archaeal actin homolog. J Mol Biol 358:145–156
Saw JH, Spang A, Zaremba-Niedzwiedzka K et al (2015) Exploring microbial dark matter to resolve the deep archaeal ancestry of eukaryotes. Philos Trans R Soc Lond Ser B Biol Sci 370:20140328
Spang A, Saw JH, Jørgensen SL et al (2015) Complex archaea that bridge the gap between prokaryotes and eukaryotes. Nature 521:173–179
van den Ent F, Amos LA, Löwe J (2001) Prokaryotic origin of the actin cytoskeleton. Nature 413:39–44
van den Ent F, Izoré T, Bharat TA, Johnson CM, Löwe J (2014) Bacterial actin MreB forms antiparallel double filaments. Elife 3:e02634
Vorobiev S, Strokopytov B, Drubin DG et al (2003) The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proc Natl Acad Sci U S A 100:5760–5765
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2017 Springer International Publishing AG
About this chapter
Cite this chapter
Lindås, AC., Valegård, K., Ettema, T.J.G. (2017). Archaeal Actin-Family Filament Systems. In: Löwe, J., Amos, L. (eds) Prokaryotic Cytoskeletons. Subcellular Biochemistry, vol 84. Springer, Cham. https://doi.org/10.1007/978-3-319-53047-5_13
Download citation
DOI: https://doi.org/10.1007/978-3-319-53047-5_13
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-53045-1
Online ISBN: 978-3-319-53047-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)