Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.6 (RNA polymerase)
 34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To assess functional relatedness of individual components of the eukaryotic transcription apparatus, three human subunits (hsRPB5, hsRPB8, and hsRPB10) were tested for their ability to support yeast cell growth in the absence of their essential yeast homologs. Two of the three subunits, hsRPB8 and hsRPB10, supported normal yeast cell growth at moderate temperatures. A fourth human subunit, hsRPB9, is a homolog of the nonessential yeast subunit RPB9. Yeast cells lacking RPB9 are unable to grow at high and low temperatures and are defective in mRNA start site selection. We tested the ability of hsRPB9 to correct the growth and start site selection defect seen in the absence of RPB9. Expression of hsRPB9 on a high-copy-number plasmid, but not a low-copy-number plasmid, restored growth at high temperatures. Recombinant human hsRPB9 was also able to completely correct the start site selection defect seen at the CYC1 promoter in vitro as effectively as the yeast RPB9 subunit. Immunoprecipitation of the cell extracts from yeast cells containing either of the human subunits that function in place of their yeast counterparts in vivo suggested that they assemble with the complete set of yeast RNA polymerase II subunits. Overall, a total of six of the seven human subunits tested previously or in this study are able to substitute for their yeast counterparts in vivo, underscoring the remarkable similarities between the transcriptional machineries of lower and higher eukaryotes.
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PMID:Six human RNA polymerase subunits functionally substitute for their yeast counterparts. 852 56

Poxvirus-encoded RNA polymerases were known previously to share extensive sequence homology in their two largest subunits with the corresponding subunits of cellular RNA polymerases and a modest alignment between the smallest poxvirus subunit and RBP10 of RNA polymerase II. The remaining subunits had no apparent cellular homologs. In this study, the HHpred program that combines amino acid sequence alignments with secondary structure predictions was used to search for homologs to the poxvirus RNA polymerase subunits. Significant matches of vaccinia RNA polymerase 22-, 19-, and 18-kDa subunits to RNA polymerase II subunits RPB5, 6, and 7, respectively, were identified. These results strengthen the concept that poxviral RNA polymerases likely evolved from cellular RNA polymerases.
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PMID:Expansion of poxvirus RNA polymerase subunits sharing homology with corresponding subunits of RNA polymerase II. 1826 49