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Example sentences for: ptgs
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Polymerization of ribonucleoside triphosphates (NTPs), which is central to a variety of crucial biological processes, including transcription, primer synthesis during DNA replication, addition of polyA tails to mRNA, addition of CCA to tRNA, uridylation in RNA editing, replication of RNA viruses, amplification of RNA in eukaryotic post-transcriptional gene silencing (PTGS), and oligoadenylate synthesis during interferon signaling, is catalyzed by a broad variety of distinct enzymes [ 1 2 3 4 ] . These polymerases belong to two major mechanistic categories, those that copy a nucleic acid template and those that are independent of a template.
Together, these results suggest that PTGS in certain oligomeric T-DNA loci is unstable and has a tendency to progress to TGS.
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.
In addition to forging a link between RNA virus resistance and PTGS, this study included a remarkably prescient model for PTGS that featured an RNA-dependent RNA polymerase (RDR), small RNAs, and dsRNA, all of which were later found to be important for the RNAi.
A second study showed that plant RNA viruses could be both initiators and targets of PTGS.
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