Words similar to thermophilic
Example sentences for: thermophilic
How can you use “thermophilic” in a sentence? Here are some example sentences to help you improve your vocabulary:
The genome of the mesophilic Halobacterium sp. contains many genes that group with the orthologs from mesophilic bacteria, whereas the majority of genes from the thermophilic archaeon Archaeoglobus fulgidus group with the orthologs from the extremely thermophilic bacteria.
Gratifyingly, many more QuartOPs supported the grouping of the thermophilic archaeon Archaeoglobus with the thermophilic bacteria Aquifex and Thermotoga . The different interdomain genome quartets that include a meso- or thermophilic archaeon are summarized in Table 3.
For example, the mesophilic euryarchaeon Halobacterium sp. has more genes in common with the mesophilic Bacteria than does the thermophilic crenarchaeote Aeropyrum pernix . However, the extremophilic euryarcheote Archaeoglobus fulgidus shares many more genes with the extremophilic bacteria, Aquifex aeolicus and Thermotoga maritima than does Halobacterium . While this example illustrates the web-like relationships among genomes, recent phylogenetic reconstructions from molecular data have explored only few alternatives to the tree-paradigm (e.g.
These include proteases in thermophilic bacteria, transcription factors, and chaperones that promote protein refolding.
The RDRPs of RNA viruses define one major lineage of nucleic acid polymerases, which additionally includes reverse transcriptases, archaeo-eukaryotic DNA polymerases, and nucleotide cyclases [ 8 9 10 11 12 13 ] . The DNA-dependent RNA polymerase of certain bacteriophages, such as T7, and the archaeo-eukaryotic primase (also detected in some bacteria) are divergent derivatives of the same fold [ 11 14 ] . The core catalytic domain of all these enzymes, the so-called "palm" domain, has an RNA-recognition motif (RRM)-like fold with strategically placed metal-coordinating residues, which form the active site [ 11 15 16 ] . In contrast, bacterial DnaG-type primases (also present in archaea and some eukaryotes) contain a polymerase domain of the Rossmann-like TOPRIM fold, which is shared with topoisomerases and OLD-family nucleases [ 17 18 19 ] . The recently solved structures of the DDRPs from yeast and the thermophilic bacterium Thermus thermophilus indicate that the β' subunit (according to the subunit nomenclature of Escherichia coli DDRP, which we hereinafter employ to designate all orthologs of the respective E. coli subunits) of these enzymes defines another distinct catalytic scaffold, which is unrelated to any of the above template-dependent RNA polymerases [ 20 21 22 23 24 ] . Additionally, the structural and evolutionary affinities of two other template-dependent RNA polymerases, namely RDRPs involved in PTGS [ 25 26 27 ] and primases of herpesviruses [ 28 ] , remain obscure.
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