EC Number   |
General Information |
Reference |
|---|
   2.7.7.56 | malfunction |
absence of RNase PH and polynucleotide phosphorylase, EC 2.7.7.8, causes growth defects. Absence of both enzymes results in the appearance and accumulation of novel mRNA degradation fragments, which are also observed in strains containing mutations in RNase R and PNPase, enzymes whose collective absence is known to cause an accumulation of structured RNA fragments. Single or double deletion of either pnp or rph had a moderate effect on the rpsO, trxA, or lpp mRNAs |
-, 722544 |
| 2.7.7.56 | malfunction |
in the absence of RNase PH, there is no 3' end trimming of 16S rRNA and no accumulation of rRNA fragments, and total RNA degradation is greatly reduced. In contrast, the degradation pattern in quality control remains unchanged when RNase PH is absent |
-, 723761 |
| 2.7.7.56 | metabolism |
RNase PH is involved in the starvation rRNA degradative pathway |
-, 723761 |
| 2.7.7.56 | more |
the core of the exosome is a versatile multisubunit RNA processing enzyme found in archaea and eukaryotes, which includes a ring of six RNase PH subunits, all six RNase PH monomers are catalytically active in the homohexameric RNase PH. Modeling of the Mth exosome RNase PH ring, overview |
721154 |
| 2.7.7.56 | physiological function |
during ribosome degradation in starving cells, RNase II regulates the amount of RNase PH present, via RNase PH stability. RNase PH normally decreases as much as 90% during starvation, in the absence of RNase II the amount of RNase PH remains relatively unchanged. In the presence of RNase II, nutrient deprivation leads to a dramatic reduction in the amount of RNase PH, thereby limiting the extent of rRNA degradation and ensuring cell survival. In the absence of RNase II, RNase PH levels remain high, leading to excessive ribosome loss and ultimately to cell death |
762370 |
| 2.7.7.56 | physiological function |
laboratory strains MG1655 and W3110 have naturally acquired the Rph-1 allele, encoding a truncated catalytically inactive RNase PH protein. Rph-1 protein inhibits RNase P-mediated 5'-end maturation of primary pre-tRNAs with leaders of less than 5 nucleotides in the absence of RppH, an RNA diphosphohydrolase. RppH is not required for 5'-end maturation of endonucleolytically generated pre-tRNAs in the Rph-1 strain and for any tRNAs in Rph mutant or Rp+x03 strains |
761382 |
| 2.7.7.56 | physiological function |
polynucleotide phosphorylase and RNase PH interact to support sRNA stability, activity, and base pairing in exponential and stationary growth conditions. They facilitate the stability and regulatory function of the sRNAs RyhB, CyaR, and MicA during exponential growth. Polynucleotide phosphorylase may contribute to pairing between RyhB and its mRNA targets. During stationary growth, each sRNA responds differently to the absence or presence of PNPase and RNase PH. Polynucleotide phosphorylase and RNase PH stabilize only Hfq-bound sRNAs |
761381 |
| 2.7.7.56 | physiological function |
role for RNase PH in the degradation of structured RNA, overview |
-, 722544 |
| 2.7.7.56 | physiological function |
the enzym eis required for the pathway of ribosomal RNA degradation during glucose starvation, not for the pathway of ribosomal RNA degradation in quality control during steady-state growth |
-, 723761 |
