RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3′ end of RNA

Substitution of the 3' terminal adenosine residue of transfer RNA in vivo.

“…The identities of the two activities are not known, but both are almost completely inhibited by 10 mM Pi, and both can synthesize runs of A residues on tRNA (data not shown). Some ofthese properties fit well with the synthetic activities of PNPase and RNase PH (19,20), but further work will be necessary to prove their identity. Whether these activities would be able to repair tRNA in vivo is also not clear.…”

Substitution of the 3' terminal adenosine residue of transfer RNA in vivo.

“…The identities of the two activities are not known, but both are almost completely inhibited by 10 mM Pi, and both can synthesize runs of A residues on tRNA (data not shown). Some ofthese properties fit well with the synthetic activities of PNPase and RNase PH (19,20), but further work will be necessary to prove their identity. Whether these activities would be able to repair tRNA in vivo is also not clear.…”

Rrp4 and Csl4 Are Needed for Efficient Degradation but Not for Polyadenylation of Synthetic and Natural RNA by the Archaeal Exosome

“…The phosphorolysis of RNA using inorganic phosphate (P i ) ions and RNA synthesis using NDPs represent the two directions of a reversible reaction catalyzed by RNase PH and the RNase PH-like core of the prokaryotic PNPase and of the archaeal exosome ,− ,, . It is known that the concentrations of P i and NDPs determine the direction of the reaction performed by RNase PH or PNPase − . The archaeal exosome is still not characterized with respect to the factors which regulate its degradative and synthetic functions.…”

Addition of Poly(A) and Heteropolymeric 3′ Ends inBacillus subtilisWild-Type and Polynucleotide Phosphorylase-Deficient Strains

“…Taken together, our data suggest strongly that an as-yet unidentified RNA polymerase, rather than PNPase, is responsible for 3Ј-end addition in B. subtilis. Although an RNase PH-encoding gene is present in B. subtilis and theoretically could be capable of adding nucleotides under low-phosphate conditions (26) on the basis of the precedent in E. coli (24), it is unlikely that this is the poly(A) polymerase of B. subtilis. It is noteworthy that the poly(A) tails associated with RNAs from mutants of S. coelicolor lacking RNase PH are indistinguishable from those associated with RNAs from wild-type strains (Bralley and Jones, unpublished).…”

Substitution of the 3' terminal adenosine residue of transfer RNA in vivo.

“…The identities of the two activities are not known, but both are almost completely inhibited by 10 mM Pi, and both can synthesize runs of A residues on tRNA (data not shown). Some ofthese properties fit well with the synthetic activities of PNPase and RNase PH (19,20), but further work will be necessary to prove their identity. Whether these activities would be able to repair tRNA in vivo is also not clear.…”

Rrp4 and Csl4 Are Needed for Efficient Degradation but Not for Polyadenylation of Synthetic and Natural RNA by the Archaeal Exosome

“…The phosphorolysis of RNA using inorganic phosphate (P i ) ions and RNA synthesis using NDPs represent the two directions of a reversible reaction catalyzed by RNase PH and the RNase PH-like core of the prokaryotic PNPase and of the archaeal exosome ,− ,, . It is known that the concentrations of P i and NDPs determine the direction of the reaction performed by RNase PH or PNPase − . The archaeal exosome is still not characterized with respect to the factors which regulate its degradative and synthetic functions.…”

Addition of Poly(A) and Heteropolymeric 3′ Ends inBacillus subtilisWild-Type and Polynucleotide Phosphorylase-Deficient Strains

“…Taken together, our data suggest strongly that an as-yet unidentified RNA polymerase, rather than PNPase, is responsible for 3Ј-end addition in B. subtilis. Although an RNase PH-encoding gene is present in B. subtilis and theoretically could be capable of adding nucleotides under low-phosphate conditions (26) on the basis of the precedent in E. coli (24), it is unlikely that this is the poly(A) polymerase of B. subtilis. It is noteworthy that the poly(A) tails associated with RNAs from mutants of S. coelicolor lacking RNase PH are indistinguishable from those associated with RNAs from wild-type strains (Bralley and Jones, unpublished).…”

Substitution of the 3' terminal adenosine residue of transfer RNA in vivo.

“…The identities of the two activities are not known, but both are almost completely inhibited by 10 mM Pi, and both can synthesize runs of A residues on tRNA (data not shown). Some ofthese properties fit well with the synthetic activities of PNPase and RNase PH (19,20), but further work will be necessary to prove their identity. Whether these activities would be able to repair tRNA in vivo is also not clear.…”

Rrp4 and Csl4 Are Needed for Efficient Degradation but Not for Polyadenylation of Synthetic and Natural RNA by the Archaeal Exosome

“…The phosphorolysis of RNA using inorganic phosphate (P i ) ions and RNA synthesis using NDPs represent the two directions of a reversible reaction catalyzed by RNase PH and the RNase PH-like core of the prokaryotic PNPase and of the archaeal exosome ,− ,, . It is known that the concentrations of P i and NDPs determine the direction of the reaction performed by RNase PH or PNPase − . The archaeal exosome is still not characterized with respect to the factors which regulate its degradative and synthetic functions.…”

Addition of Poly(A) and Heteropolymeric 3′ Ends inBacillus subtilisWild-Type and Polynucleotide Phosphorylase-Deficient Strains

“…Taken together, our data suggest strongly that an as-yet unidentified RNA polymerase, rather than PNPase, is responsible for 3Ј-end addition in B. subtilis. Although an RNase PH-encoding gene is present in B. subtilis and theoretically could be capable of adding nucleotides under low-phosphate conditions (26) on the basis of the precedent in E. coli (24), it is unlikely that this is the poly(A) polymerase of B. subtilis. It is noteworthy that the poly(A) tails associated with RNAs from mutants of S. coelicolor lacking RNase PH are indistinguishable from those associated with RNAs from wild-type strains (Bralley and Jones, unpublished).…”