Domain Archaea
Phylogenetic overview
-
Comparative sequence analysis of 16S RNA molecules has
elucidated that life on Earth is of 3 primary lineages (referred to as
domains):
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(i) Eukarya
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(ii) Bacteria
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(iii)Archaea
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Kingdom Crenarchaeota: mainly hyperthermophiles
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Kingdom Euryarchaeota: methanogens, halophiles, Thermoplasma
& Archaeoglobus
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Kingdom Korarchaeota: based on 16S rRNA sequences from
uncultured microbes from terrestrial hot springs

Structural distinction between the
domains
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Cell Walls
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Bacterial = peptidoglycan
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Archaeal = pseudopeptidoglycan, or protein only
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Eukaryal = plants (polysaccharide), animals (none), fungi
(chitin)
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Cell Membranes
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Bacterial and eucaryal lipids = straight chain fatty acids
linked to glycerol molecules by ester linkages
-
Archael lipids = branched chain hydrocarbons linked to
glycerol molecules by ether linkages - fatty acid components are not found
in archeal lipids
Detailed description on this section is available from
the Microbiology subject (SS12BMI). Microbial structures and their functions
in Bacteria, Archaea and Eucarya.
Molecular Biology comparisons
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Genome organisation
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Similar to bacteria
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Chromosome is a single, circular DNA molecule
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Extrachromosomal elements (eg plasmids) are found in archaea
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Genomic resistance to thermal denaturation & genomic
structural intergrity in extreme thermophiles is related to:
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high intracellular salt concentrations (solutes)
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DNA binding proteins (aka Histone-like proteins similar
to Eucarya):
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MC1 : Methanosarcinaceae
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HMf: Methanobacteriales
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share amino acid homology to Eucaryal Histone proteins
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organization of DNA in chromatin-like structure
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histone + Eucarya DNA = negative supercoiling & nucleosome
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HMf + Archaea DNA = positive supercoiling
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HTa: Thermoplasma
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HTa-like: Sulfolobus
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DNA Replication
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Archael DNA polymerases have been identified with primary
protein sequences resembling polymerases from eukaryotes, eukaryal viruses
and E.coli
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Some posses 3'-5' exonuclease (or proofreading) activity
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A Halobacterium halobium polymerase / primase has
been identified with reverse transcriptase activity
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Topoisomerases, gyrase and restriction endonucleases have
also been identified in Archaea
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Transcription
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Archael RNA polymerases are complex, consisting of up
tp 14 subunits (c.f. 4 in E.coli)
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Comparative sequence homology of genes encoding subunits
suggests that the polymerase is more closely related to eukaryal polymerases
than bacterial
-
Unlike, E.coli RNA polymerase, Archael RNA polymerases
are unable to initiate transcription in vitro; This is also seen in eukaryotes
where general transcription factors are required for initiation
-
Archael promoters have an A-T rich sequence at -32 to
-25 bp upstream of the transcriptional start: the consensus sequence resembles
a eukaryotic TATA box
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Gene Organisation
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Primary sequence of archael proteins more often resemble
eukaryotic homologues than bacterial ones
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Functionally related genes are often organised in operon
like structures
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Introns have been found in archael 23S and 16S rRNA and
tRNA genes
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Varying arrangements of genes can be seen in Archaea
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Methyl coenzyme M reductase, RNAP and bacterio-opsin genes
are good examples
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Translation
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Translation signals resemble those found in bacteria (i.e.
there are short regions of complementarity between the 5' end of the mRNA
and the 3' end of the 16S rRNA)
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Cloning and Expression
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Cloning usually follows protein-purification using standard
molecular biology techniques
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Expression in heterologous hosts may be complcated by
the altered environment in which expression is occuring and differences
in translation and post-translational mechanisms
References:
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Madigan, M.T., Martinko, J.M. and Parker, J. Brock, Biology
of Microorganisms, Prentice Hall, 8th Edition, 1997
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M.Ciaramella et al, Molecular biology of extremophiles,
World Journal of Microbiology and Biotechnology, Vol 11, pp 71-84, 1995
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Danson et al., Archaebacteria, Biochemistry and Biotechnology,
London: Biochemical Society, 1992
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Brown, J.W. et al, Gene Structure, Organisation and Expression
in Archaebacteria. CRC Critical Reviews in
Microbiology, Vol 16, No. 4, 1989
Author: Dr Bharat Patel <bharat@trishul.sci.gu.edu.au>
[Created 14 Sept 1995]
[Modified 27 Aug 1997]