Words similar to bacteriophages
Example sentences for: bacteriophages
How can you use “bacteriophages” in a sentence? Here are some example sentences to help you improve your vocabulary:
Recently, data obtained from genome sequencing projects have made it clear that bacteria exchange genetic information by means of transducing bacteriophages, conjugative plasmids, and natural transformation [ 18 ] at a much higher rate than previously thought [ 19 ] . There seem to be few insurmountable barriers to interspecies gene transfer, with transfers being documented between such diverse organisms as archea and eubacteria [ 20 ] . Synechococcus sp. [ 21 ] and some P. stutzeri strains [ 22 ] are two examples of the many bacterial species known to undergo natural transformation.
The classic helix-turn-helix (HTH)-domain proteins, which govern the switch between the lysogenic and lytic pathways of temperate bacteriophages, and repressors containing the MetJ/Arc domain are well-known examples of such regulatory DNA-binding proteins in prokaryotic virus-host systems [ 4, 5, 6, 7, 8].
The majority of the domains with which the KilA-N and Bro-N domains combine in multidomain proteins are restricted to proteins encoded by temperate bacteriophages and large eukaryotic DNA viruses (the exceptions are a few domains that are common in cellular proteomes, such as HTH, CCCH and RING finger).
The Pal lineage of the NIpC-like orthologous group is restricted to the bacteriophages and their prophage remnants in Gram-positive bacteria.
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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