Words similar to transcriptases
Example sentences for: transcriptases
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This scenario shows parallels to the probable evolutionary history of another major, unrelated class of polymerases, the RDRPs and reverse transcriptases containing the palm domain.
The hepadnaviral P protein possesses many unique features relative to the better studied reverse transcriptases of the retroviruses: (i) it uses its own amino-terminal domain as a protein primer for initiation of DNA synthesis [ 7, 9, 10], (ii) it cannot be isolated in an active form from virions without partial proteolysis or denaturation [ 13, 14, 15], and (iii) under normal circumstances it is active only on the endogenous pregenomic RNA that is encapsidated with it in the viral cores [ 16].
The classical adenylyl cyclases, guanylyl cyclases and the GGDEF (diguanylate cyclase) domains share the catalytic palm domain with the family B DNA polymerases, reverse transcriptases, viral RNA dependent RNA polymerases and eukaryote-type primases [ 4 13 14 ] . The pathogenic adenylyl cyclases of several bacteria and the CyaA-like proteobacteria adenylyl cyclases are extremely divergent versions of the catalytic domain seen in the Pol-β family of nucleotidyl transferases [ 15 ] (also see SCOP database: http://scop.mrc-lmb.cam.ac.uk/scop/).
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.
The two enzymatic active sites of DHBV P are likely to interact with the viral nucleic acids through a single binding interaction because they are very close to each other and because other reverse transcriptases (such as that of HIV) bind to the RNA:DNA heteroduplex as a single protein entity [ 32].
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