Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius

Green, George R.; Searcy, Dennis G.; DeLange, Robert J.

doi:10.1016/0167-4781(83)90066-0

Cited by 54 publications

(19 citation statements)

References 25 publications

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“…(1) It has a histone, which functions to protect the DNA from heat [13]. Simple histone-like proteins occur throughout the Archaea, but are particularly well developed in the thermophilic species [14][15][16]. (2) T. acidophilum has no cell wall, and instead has a well-developed cytoskeleton [17].…”

Section: Ancestors Of Nucleocytoplasm and Of Mitochondriamentioning

confidence: 99%

Metabolic integration during the evolutionary origin of mitochondria

Searcy

2003

Cell Res

115

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Although mitochondria provide eukaryotic cells with certain metabolic advantages, in other ways they may be disadvantageous. For example, mitochondria produce reactive oxygen species that damage both nucleocytoplasm and mitochondria, resulting in mutations, diseases, and aging. The relationship of mitochondria to the cytoplasm is best understood in the context of evolutionary history. Although it is clear that mitochondria evolved from symbiotic bacteria, the exact nature of the initial symbiosis is a matter of continuing debate. The exchange of nutrients between host and symbiont may have differed from that between the cytoplasm and mitochondria in modern cells. Speculations about the initial relationships include the following.(1) The pre-mitochondrion may have been an invasive, parasitic bacterium. The host did not benefit. (2) The relationship was a nutritional syntrophy based upon transfer of organic acids from host to symbiont. (3) The relationship was a syntrophy based upon H2 transfer from symbiont to host, where the host was a methanogen. (4) There was a syntrophy based upon reciprocal exchange of sulfur compounds. The last conjecture receives support from our detection in eukaryotic cells of substantial H2S-oxidizing activity in mitochondria, and sulfur-reducing activity in the cytoplasm.

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Section: Ancestors Of Nucleocytoplasm and Of Mitochondriamentioning

confidence: 99%

Metabolic integration during the evolutionary origin of mitochondria

Searcy

2003

Cell Res

115

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“…A small, abundant DNA-binding protein, denoted Sac10b, was first isolated from S. acidocaldarius in the mid-80s [56]. Later, homologs of Sac10b were found to be highly conserved among Archaea and make up the Sac10b protein family (Figure 1) [57].…”

Section: The Sac10b Protein Family (Alba)mentioning

confidence: 99%

Archaeal chromatin proteins

Zhang

Guo

Huang

2012

Sci. China Life Sci.

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Archaea, along with Bacteria and Eukarya, are the three domains of life. In all living cells, chromatin proteins serve a crucial role in maintaining the integrity of the structure and function of the genome. An array of small, abundant and basic DNA-binding proteins, considered candidates for chromatin proteins, has been isolated from the Euryarchaeota and the Crenarchaeota, the two major phyla in Archaea. While most euryarchaea encode proteins resembling eukaryotic histones, crenarchaea appear to synthesize a number of unique DNA-binding proteins likely involved in chromosomal organization. Several of these proteins (e.g., archaeal histones, Sac10b homologs, Sul7d, Cren7, CC1, etc.) have been extensively studied. However, whether they are chromatin proteins and how they function in vivo remain to be fully understood. Future investigation of archaeal chromatin proteins will lead to a better understanding of chromosomal organization and gene expression in Archaea and provide valuable information on the evolution of DNA packaging in cellular life.Archaea, chromatin protein, biochemical properties, structure, post-translational modification Citation:

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“…Another unexplored area is the stability of the nucleic acids, e. g. the maintenance of the double helical structure, at the very high growth temperatures. Some stabilization could be obtained by basic DNA binding proteins (Thomm et al, 1982;Green et al, 1983) or by introduction of positive superhelical strains into DNA by a reverse gyrase (Kikuchi and Asai, 1984). The thermostability of DNA could also be improved by an increased GC-content (Marmur and Doty, 1962), but no correlation has been found between the GC-content of DNA and the growth temperature of extremely thermophilic S0-metabolizers (Table 4).…”

Section: Prerequisites and Limits Of Extremely Thermophilic Lifementioning

confidence: 99%

Extremely thermophilic sulfur-metabolizing archaebacteria

Stetter

Segerer

Zillig

et al. 1986

Systematic and Applied Microbiology

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SummaryVarious extremely thermophilic coccoid, rod-or plate-shaped S0-metabolizing archaebacteria exhibit optimum growth at above 80 °C. Pyrodictium is the most thermophilic of these organisms, growing at temperatures of up to 110°C and exhibiting optimum growth at about 105 °C. All of these organisms proliferate on the basis of diverse types of anaerobic and aerobic lithoautotrophy and heterotrophy.

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Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius

Cited by 54 publications

References 25 publications

Metabolic integration during the evolutionary origin of mitochondria

Metabolic integration during the evolutionary origin of mitochondria

Archaeal chromatin proteins

Extremely thermophilic sulfur-metabolizing archaebacteria

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