Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.7.8 (
polynucleotide phosphorylase
)
723
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
RNA-
OUT
, the 69-nucleotide antisense RNA that regulates Tn10/IS10 transposition folds into a simple stem-loop structure. The unusually high metabolic stability of RNA-
OUT
is dependent, in part, on the integrity of its stem-domain: mutations that disrupt stem-domain structure (Class II mutations) render RNA-
OUT
unstable, and restoration of structure restores stability. Indeed, there is a strong correlation between the thermodynamic and metabolic stabilities of RNA-
OUT
. We show here that stem-domain integrity determines RNA-
OUT
's resistance to 3' exoribonucleolytic attack: Class II mutations are almost completely suppressed in Escherichia coli cells lacking its principal 3' exoribonucleases, ribonuclease II (RNase II) and
polynucleotide phosphorylase
(
PNPase
). RNase II and
PNPase
are individually able to degrade various RNA-
OUT
species, albeit with different efficiencies: RNA-
OUT
secondary structure provides greater resistance to RNase II than to
PNPase
. Surprisingly, RNA-
OUT
is threefold more stable in wild-type cells than in cells deficient for RNase II activity, suggesting that RNase II somehow lessens
PNPase
attack on RNA-
OUT
. We discuss how this might occur. We also show that wild-type RNA-
OUT
stability changes only two-fold across the normal range of physiological growth temperatures (30-44 degrees C) in wild-type cells, which has important implications for IS10 biology.
...
PMID:Decay of the IS10 antisense RNA by 3' exoribonucleases: evidence that RNase II stabilizes RNA-OUT against PNPase attack. 753 7