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double-stranded RNA + H2O
5'-phosphooligonucleotides
responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
R1.1 RNA + H2O
?
internally 32P-labeled R1.1
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
double-stranded RNA + H2O
?
-
R1.1 RNA
-
-
?
ds-rRNA + H2O
mature ds-rRNA
dsRNA + H2O
?
-
RNase III(E38A) generates discrete-sized products from long dsRNA
-
-
?
dsRNA + H2O
processed RNA
hairpin RNA R1.1 + H2O
?
-
RNase III(E38A) cleaves at the primary site and remains bound to the RNA, thereby preventing cleavage at the secondary site
-
-
?
mRNA transcripts + H2O
5'-phosphooligonucleotides
poly(A)-poly(U) + H2O
5'-phosphooligonucleotides
-
-
-
-
?
pre-16S rRNA + H2O
mature 16S rRNA
-
-
-
-
?
pre-23S rRNA + H2O
mature 23S rRNA
-
-
-
-
?
pre-5S rRNA + H2O
mature 5S rRNA
-
-
-
-
?
pre-mRNA + H2O
mature mRNA
pre-rRNA + H2O
mature rRNA
-
-
-
-
?
R1.1 RNA + H2O
2 fragment of R1.1 RNA
-
substrate is enzymatically synthesized based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, 1 cleavage site
-
-
?
R1.1 RNA + H2O
2 fragments of R1.1 RNA
R1.1 RNA + H2O
?
-
-
-
-
?
R1.1 RNA + H2O
fragments of R1.1 RNA
R1.1 RNA derivatives + H2O
fragments of R1.1 RNA
-
based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, derivative R1.1[CL3B] is not cleaved and its binding to the enzyme leads to uncoupling of substrate recognition and cleavage
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
RNA precursor + H2O
mature RNA
-
phage lambda RNA, enzyme is involved in translation control
-
-
?
RNA substituted with guanosine 5'-O-(1-thiotriphosphate) + H2O
5'-phosphooligonucleotides containing guanosine 5'-O-(1-thiotriphosphate)
-
cleavage specificity is not altered by modified RNA
-
-
?
single-stranded RNA + H2O
5'-phosphooligonucleotides
tRNA + H2O
5'-phosphooligonucleotides
additional information
?
-
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
15 bases in average
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
bacteriophage T7 RNA
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
bacteriophage T7 RNA
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
no activity on DNA-RNA hybrids
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
cleaves multimeric tRNA precursor at the spacer region, also involved in processing of precursor rRNA, hnRNA and early T7-mRNA. Also cleaves double-stranded DNA and single-stranded RNA
134334, 134335, 134336, 134337, 134338, 134339, 134340, 134341, 134342, 134343, 134345, 134346, 134348, 134349, 134351, 134352, 134353, 134354, 134357, 134358, 134359, 134360, 134361, 134362, 134364, 134365 -
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
Dicer is a multidomain ribonuclease that processes double-stranded RNAs (dsRNAs) to 21 nt small interfering RNAs (siRNAs) during RNA interference, and excises microRNAs from precursor hairpins. Dicer contains two domains related to the bacterial dsRNA specific endonuclease, RNase III, which is known to function as a homodimer. Enzyme has only one processing center, containing two RNA cleavage sites and generating products with 2 nt 3' overhangs. It is proposed that Dicer functions through intramolecular dimerization of its two RNase III domains, assisted by the flanking RNA binding domains, PAZ and dsRBD
-
-
?
ds-rRNA + H2O
mature ds-rRNA
-
-
-
-
?
ds-rRNA + H2O
mature ds-rRNA
-
double-strand RNA specific endonuclease
-
-
?
dsRNA + H2O
mature RNA
-
-
-
-
?
dsRNA + H2O
mature RNA
-
enzyme is involved in the maturation and decay of cellular, phage and plasmid RNAs
-
-
?
dsRNA + H2O
mature RNA
-
enzyme plays a key role in diverse maturation and degradation processes
-
-
?
dsRNA + H2O
mature RNA
-
obligatory step in the maturation and decay of diverse RNAs
-
-
?
dsRNA + H2O
mature RNA
-
reshaping of fully or partially double-stranded RNA precursors into mature RNAs involved in pre-mRNA splicing, RNA modification, translation, gene silencing, and regulation of developmental timing
-
-
?
dsRNA + H2O
mature RNA
-
cleavage of fully or partially double-stranded RNA precursors into mature structural and catalytic RNAs such as the snRNAs that splice pre-mRNA, rRNAs, and tRNAs that function in translation, swnoRNAs that guide modificatin of rRNAs, and individual mRNAs, whose expression they regulate
staggered breaks with 2 nt, 3'-overhanging ends and 5'-phosphate and 3'-hydroxy termini
-
?
dsRNA + H2O
mature RNA
-
double-strand RNA-specific, the dsRNA-binding domain is important for substrate binding but not for catalytic activity, while the catalytic domain is important for catalytic activity but not for substrate binding
-
-
?
dsRNA + H2O
mature RNA
-
one functional monomer is sufficient for cleavage activity of the dimer
-
-
?
dsRNA + H2O
processed RNA
-
-
-
-
?
dsRNA + H2O
processed RNA
-
specific for double-stranded RNA
enzyme produces 12-15 base pair duplex products with 5'-phosphate, 3'-hydroxyl termini
-
?
mRNA transcripts + H2O
5'-phosphooligonucleotides
-
reduces expression of itself
-
-
?
mRNA transcripts + H2O
5'-phosphooligonucleotides
-
mRNA phage SP82 is not cleaved by E. coli RNase III
-
-
?
mRNA transcripts + H2O
5'-phosphooligonucleotides
-
RNAI, a regulator of plasmid replication is cleaved
-
-
?
mRNA transcripts + H2O
5'-phosphooligonucleotides
-
to affect gene expression
-
-
?
pre-mRNA + H2O
mature mRNA
-
-
-
-
?
pre-mRNA + H2O
mature mRNA
-
enzyme regulates gene expression by controlling mRNA translation and stability
-
-
?
R1.1 RNA + H2O
2 fragments of R1.1 RNA
-
substrate is enzymatically synthesized based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, 1 cleavage site
-
-
?
R1.1 RNA + H2O
2 fragments of R1.1 RNA
-
substrate is enzymatically synthesized based on the R1.1 processing signal, which is encoded in the phage T7 genetic early regionbetween genes 1.0 and 1.1, 1 cleavage site
-
-
?
R1.1 RNA + H2O
fragments of R1.1 RNA
-
based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, recombinant substrate from in vitro transcription, determination of cleaving positions for the recombinant hybrid enzyme mutants
-
-
?
R1.1 RNA + H2O
fragments of R1.1 RNA
-
based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, several derivatives containing an internal loop
product determination
-
?
R1.1 RNA + H2O
fragments of R1.1 RNA
-
based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, substrate possesses 2 ethidium bromide binding sites in the internal loop and the lower stem, respectively, both consisting of an A-A pair stacked on a CG pair, which is a motif that is a favourable environment for intercalation
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
-
-
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
-
no activity on 23S RNA and 16S RNA
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
-
the small and stable 10Sa RNA is cleaved
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
-
7S RNA is cleaved
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
-
23S RNA in Rhodobacter capsulatus
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
-
initiates maturation of 23S and 16S RNA species
-
-
?
single-stranded RNA + H2O
5'-phosphooligonucleotides
-
-
-
-
?
single-stranded RNA + H2O
5'-phosphooligonucleotides
-
E. coli infected with bacteriophage T4 deletion mutant
-
-
?
tRNA + H2O
5'-phosphooligonucleotides
-
-
-
-
?
tRNA + H2O
5'-phosphooligonucleotides
-
no activity on yeast tRNA
-
-
?
tRNA + H2O
5'-phosphooligonucleotides
-
initiates maturation of phage T4 tRNA
-
-
?
tRNA + H2O
5'-phosphooligonucleotides
-
five additional secondary cleavage sites in RNA A3t from bacteriophage T7
-
-
?
additional information
?
-
as a binding protein, RNase III binds and stabilizes certain RNAs, thus suppressing the expression of certain genes
-
-
?
additional information
?
-
identification of the cleavage targets of the endonucleolytic enzyme at a transcriptome-wide scale and delineation of its in vivo cleavage rules, overview. Usage of tailored RNA-seq-based technology, which allows transcriptome-wide mapping of RNase III cleavage sites at a nucleotide resolution establishing a cleavage pattern of a double cleavage in an intra-molecular stem structure, leaving 2-nt-long 3' overhangs, and refines the base-pairing preferences in the cleavage site vicinity. The two stem positions between the cleavage sites are highly base-paired, usually involving at least one G-C or C-G base pair. A clear distinction between intra-molecular stem structures that are RNase III substrates and intra-molecular stem structures randomly selected across the transcriptome, emphasizing the in vivo specificity of RNase III
-
-
?
additional information
?
-
bdm, corA, mltD, proU, betT, and proP mRNAs are used as RNase III substrates, cleavage site determination reveals that no distinct consensus sequences, which would account for the specificity of RNase III recognition and cleavage process, are observed when in vivo RNase III substrates are analyzed
-
-
?
additional information
?
-
-
bdm, corA, mltD, proU, betT, and proP mRNAs are used as RNase III substrates, cleavage site determination reveals that no distinct consensus sequences, which would account for the specificity of RNase III recognition and cleavage process, are observed when in vivo RNase III substrates are analyzed
-
-
?
additional information
?
-
identification of RNase III cleavage sites and generation of a map of the cleavage sites in both intra-molecular and intermolecular duplex substrates. The recognition of DC targets by RNase III is highly specific
-
-
?
additional information
?
-
predicted secondary structure of substrates' RNase III sites, overview
-
-
?
additional information
?
-
ribonuclease III site-specifically cleaves double-stranded(ds) structures in diverse cellular, plasmid and phage RNAs. The catalytic sites employ Mg2+ ions to hydrolyze phosphodiesters, providing products with two-nucleotide, 3'-overhangs and 5'-phosphomonoester, 3'-hydroxyl termini
-
-
?
additional information
?
-
-
ribonuclease III site-specifically cleaves double-stranded(ds) structures in diverse cellular, plasmid and phage RNAs. The catalytic sites employ Mg2+ ions to hydrolyze phosphodiesters, providing products with two-nucleotide, 3'-overhangs and 5'-phosphomonoester, 3'-hydroxyl termini
-
-
?
additional information
?
-
-
involved in the maturation of the ribosomal RNA precursor, and bacteriophage T7 mRNA precursors, enzyme participates in the degradation as well as maturation of diverse cellular, phage, and plasmid RNAs
-
-
?
additional information
?
-
-
no activity with (rA)25, (rU)25, (rC)25, dsDNA, ssDNA and an RNA-DNA hybrid
-
-
?
additional information
?
-
-
RNA structure-dependent uncoupling of substrate recognition and cleavage, in vitro selection and structure determination of cleavage resistant variants of T7 R1.1 RNA classes I and II, due to altered conformation, overview
-
-
?
additional information
?
-
-
specificity for A-form dsRNA, enzyme is loosely associated with ribosomes
-
-
?
additional information
?
-
-
substrate specificity of the recombinant hybrid enzyme mutants, substrate specificity is determined by the catalytic N-terminus of the enzyme
-
-
?
additional information
?
-
-
substrate specificity with diverse RNA mutant substrate variants, the RNA internal loop, in which is located the required single scissile phosphodiester, is the reactivity epitope the substrates, overview
-
-
?
additional information
?
-
-
cleaves internally 32P-labeled R1.1(WC) RNA
-
-
?
additional information
?
-
-
substrate is bdm mRNA with recombinant His-tagged RNase III. Introduction of random mutations at the RNase III cleavages sites in bdm mRNA alter the enzyme activity, secondary structures and the stability of hairpins containing the RNase III cleavage sites 3 and 4-II, and RNase II cleavage patterns, overview
-
-
?
additional information
?
-
-
RNase III is a double-stranded RNA-specific endoribonuclease that processes and degrades numerous mRNA molecules in Escherichia coli, it acts on mltD mRNA, which encodes membrane-bound lytic murein transglycosylase D. Introduction of a nucleotide substitution at the identified RNase III cleavage sites inhibited RNase III cleavage activity on mltD mRNA, resulting in, consequently, approximately two-fold increase in the steady-state level of the mRNA
-
-
?
additional information
?
-
-
RNase III specifically processes the proU mRNA within a conserved secondary structure extending from position +203 to +293 of the transcript
-
-
?
additional information
?
-
-
the enzyme cleaves the proU operon transcript reducing its half-life from 65 sec to 4 sec, the rapid degradation ensures efficient inhibition of proU expression and further uptake of osmoprotectants. Processing of dsRNA, product release is the rate-limiting step in the catalytic pathway
-
-
?
additional information
?
-
-
the enzyme processes betT and proU mRNA
-
-
?
additional information
?
-
-
the enzyme processes ribosomal RNA
-
-
?
additional information
?
-
-
the enzyme cleaves betT and proU mRNA. Introdution of nucleotide substitutions C33U and C39U in thhe enzymes' cleavage sites of betT mRNA inhibit the enzyme activity
-
-
?
additional information
?
-
the enzyme is active with DAPI-enriched pre-rRNA fragments
-
-
?
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evolution
RNase III is a member of the phylogenetically highly conserved endoribonuclease III family
malfunction
pyruvate dehydrogenase activity is increased in an rnc deletion mutant compared to the wild-type strain in early stationary phase, confirming the link between RNA turnover and regulation of pathway activity
malfunction
the YmdB R40A mutation causes a 16fold increase in KD, and the D128A mutation in both RNase III subunits (D128A/D1280A) causes an 83fold increase in KD
metabolism
influence of different RNase activities, including RNase III, on central metabolism, overview
metabolism
RNase III plays a key role in posttranscriptional regulatory pathways in Escherichia coli. RNase III-mediated regulation of environmental stress-related genes provide evidence of the critical role of RNase III in rapid cellular responses to various stress conditions. Although regulation of such genes by RNase III is essential for bacteria to adapt to a wide range of environmental conditions that they encounter in nature, the exact mode of substrate recognition and mechanisms underlying the regulation of RNase III activity is not fully understood, RNase III activity during various environmental stresses, overview. Mechanisms of RNase III-mediated regulation of a subgroup of mRNA species including bdm, betT, proP, and proU whose protein products are associated with the cellular response to osmotic stress
physiological function
bacterial RNase III plays important roles in the processing and degradation of RNA transcripts. A clear distinction between intramolecular stem structures that are RNase III substrates and intra-molecular stem structures randomly selected across the transcriptome, emphasizing the in vivo specificity of RNase III
physiological function
ribonuclease III (RNase III) is a conserved, gene-regulatory bacterial endonuclease that cleaves double-helical structures in diverse coding and noncoding RNAs. RNase III is subject to multiple levels of control, reflective of its global regulatory functions. Escherichia coli (Ec) RNase III catalytic activity is known to increase during bacteriophage T7 infection, reflecting the expression of the phage-encoded protein kinase, T7PK. Primary substrate for RNase III is the 5500 nt transcript of the rRNA operons, containing the 16S, 23S and 5S rRNAs, with the enzyme acting co-transcriptionally to provide the immediate precursors to the mature rRNAs8. RNase III also can determine mRNA half-life by catalyzing the rate-limiting cleavage step in the decay pathway. Double-helical structures that are formed by binding of small noncoding RNAs (sRNAs) provide RNase III targets, and regulate mRNA translation and/or stability. The diversity of RNase III targets and the multiple actions of the enzyme in conjunction with sRNAs and other factors underscore the global regulatory function of RNase III
physiological function
RNase III is a widespread endoribonuclease that binds and cleaves double-stranded RNA in many critical transcripts. RNase III cleavage at additional sites found in RNA of genes aceEF, proP, tnaC, dctA, pheM, sdhC, yhhQ, glpT, aceK, and gluQ accelerate RNA decay, consistent with previously described targets wherein RNase III cleavage initiates rapid degradation of secondary messages by other RNases. In contrast, cleavage at three sites in the ahpF, pflB, and yajQ transcripts lead to stabilized secondary transcripts. Two other sites in hisL and pheM overlap with transcriptional attenuators that likely serve to ensure turnover of these highly structured RNAs. Many of the additional RNase III target sites are located on transcripts encoding metabolic enzymes, while two RNase III sites are located within transcripts encoding enzymes near a key metabolic node connecting glycolysis and the tricarboxylic acid (TCA) cycle
physiological function
RNase III plays a role in rRNA and tRNA maturation in Escherichia coli. RNase III enzymatic activity can be regulated on multiple levels that include autoregulation by cleavage of its own mRNA message. The primary 30S rRNA transcript, which includes all of the rRNA genes, is cleaved by RNase III within the flanking double-stranded regions. This generates the 17S precursor of the 16S rRNA and the p23S precursor of the 23S rRNA. RNase III-mediated regulation of environmental stress-related genes provide evidence of the critical role of RNase III in rapid cellular responses to various stress conditions. Although regulation of such genes by RNase III is essential for bacteria to adapt to a wide range of environmental conditions that they encounter in nature, the exact mode of substrate recognition and mechanisms underlying the regulation of RNase III activity is not fully understood, RNase III activity during various environmental stresses, overview. Osmoregulation of RNase III activity, the osmoregulatory K+ uptake is mediated by the Trk and Kdp transporters. Analysis of substrate RNA molecules bound to RNase III by in vivo crosslinking and immunoprecipitation of RNase III indicated that downregulation of RNase III cleavage activity under hyperosmotic stress is caused by the decreased RNA binding capacity of RNase III. Autoregulation, Modulation of RNase III activity induced by antibiotic stress. RNase III can also be regulated by trans-acting factors, e.g. YmdB. T7 protein kinase positively regulates RNase III in Escherichia coli
physiological function
the complex posttranscriptional regulation mechanism of the Escherichia coli pnp gene, which encodes the phosphorolytic exoribonuclease polynucleotide phosphorylase (PNPase), involves two endoribonucleases, namely, RNase III and RNase E, and PNPase itself, which thus autoregulates its own expression. Autogenous regulation of Escherichia coli PNPase via translational repression is RNase III-independent. The target of PNPase is a mature pnp mRNA previously processed at its 5' end by RNase III, rather than the primary pnp transcript (RNase III-dependent models). PNPase also regulates its own expression via a reversible RNase III-independent pathway acting upstream from the RNase III-dependent branch. This pathway requires the PNPase RNA binding domains KH and S1 but not its phosphorolytic activity. The RNase III-independent autoregulation of PNPase seem to occur at the level of translational repression, possibly by competition for pnp primary transcript between PNPase and the ribosomal protein S1
evolution
-
class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as RNase III in Escherichia coli. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains
evolution
-
the enzyme belongs to the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. RNase III family members share a unique fold (RNase III domain) that can dimerize to form a structure that binds dsRNA and cleaves phosphodiesters on each strand, providing the characteristic 2 nt, 3'-overhang product ends. Domain structures of ribonuclease III family polypeptides, overview
malfunction
-
the rnc RNase III mutant strain has reduced levels of one of the full-length GadY-dependent bands. However, this mutant does not abolish processing, indicating redundancy with respect to enzymes capable of catalyzing GadY-directed processing
malfunction
-
blocking of RNase III processing by mutation of the processing site eliminates post-transcriptional osmoregulation of proU
malfunction
gene rnc deletion mutants are slow in rRNA operon induction and synthetically lethal with gene fis, encoding the transcriptional regulator Fis. In the absence of RNase III, not only the double pre-rRNP length gradient is lost but also the relative RNA polymerase occupancy in the spacer and nonspacer regions are approximately similar
metabolism
-
the RNase III-mediated regulatory pathway functions to modulate corA expression and, in turn, the influx of metal ions transported by CorA in Escherichia coli
metabolism
-
two tandem RNase III cleavage sites determine betT mRNA stability in response to osmotic stress. The betT gene forms part of the osmoregulatory system Bet regulon, which participates in the synthesis of glycine betaine from externally supplied choline. BetT protein belongs to the betaine-choline-carnitine transporter family. The enzyme affects also the choline-uptake proU transporter system
physiological function
-
base pairing of the GadY small RNA with the intergenic region of the gadX-gadW mRNA results in directed processing events within the region of complementarity. Multiple enzymes are involved in the GadYdirected cleavage including the double-strand RNA-specific endoribonuclease RNase III, mechanism of regulation, overview
physiological function
-
enzyme RNase III cleavage at A and B sites of mltD mRNA regulates mltD degradation,
physiological function
-
processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs. RNase III is negatively regulated by the macrodomain protein, YmdB, and might be dependent upon the direct interaction of the two proteins. The enzyme's catalytic activity is also subject to positive regulation. The T7 bacteriophage expresses a protein kinase that phosphorylates RNase III and enhances catalytic activity about fourfold, as measured in vitro
physiological function
-
the enzyme negatively regulates the expression of betT, the cleavage determines betT mRNA stability in vivo, osmoregulation of betT expression by RNase III
physiological function
the enzyme plays a role in the rapid induction of ribosomal operons during outgrowth and is essential in the absence of the transcriptional regulator Fis, suggesting a linkage of transcription and RNA processing for ribosomal operons in Escherichia coli, the enzyme has an effect on ribosome operon transcription and is involved in the early process steps of rRNA biogenesis, overview The enzyme is required for localization of the 5 pre-rRNA leader to the nucleoid and for optimal induction of rRNA synthesis. RNase III processing of pre-rRNA occurs cotranscriptionally
physiological function
-
the enzyme RNase III initiates rapid degradation of proU mRNA upon hypoosmotic stress, osmoregulation occurs at a post-transcriptional level. Upon osmotic downshift, the enzyme immediately processes the proU mRNA which reduces its half-life from 65 sec to less than 4 sec
physiological function
-
the steady-state levels of metal transporter corA mRNA as well as the degree of cobalt influx into the cell are dependent on cellular concentrations of the enzyme RNase III. Enzyme RNase III cleavage constitutes a rate-determining step for corA mRNA degradation, downregulation of corA expression by the enzyme, overview. Introduction of point mutations in RNase III cleavage sites C-122G, U-153A, and A-152G of corA mRNA abolishes the enzyme cleavage activity on corA mRNA and results in prolonged half-lives of the mRNA
additional information
complex formation of ribonuclease III with the regulatory macrodomain protein, YmdB, protein-protein docking and interaction analysis by homology modelling (using the Escherichia coli RNase III homodimer as template, PDB entry 1SPV, 2.0 A resolution) and surface plasmon resonance (SPR) analysis, kinetic and thermodynamic values for the YmdB-RNase III interaction, and the effect of specific mutations, overview. Interaction of the conserved YmdB residue R40 with specific RNase III residues at the subunit interface
additional information
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complex formation of ribonuclease III with the regulatory macrodomain protein, YmdB, protein-protein docking and interaction analysis by homology modelling (using the Escherichia coli RNase III homodimer as template, PDB entry 1SPV, 2.0 A resolution) and surface plasmon resonance (SPR) analysis, kinetic and thermodynamic values for the YmdB-RNase III interaction, and the effect of specific mutations, overview. Interaction of the conserved YmdB residue R40 with specific RNase III residues at the subunit interface
additional information
Ec-RNase III homology-modeled structure in complex with cleaved dsRNA, overview
additional information
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Ec-RNase III homology-modeled structure in complex with cleaved dsRNA, overview
additional information
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structure analysis and comparison to other enzyme family members, overview
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