3.1.26.3: ribonuclease III
This is an abbreviated version!
For detailed information about ribonuclease III, go to the full flat file.
Word Map on EC 3.1.26.3
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3.1.26.3
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rnai
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argonaute
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drosophila
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germline
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rna-induced
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viruses
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duplex
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ovarian
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microprocessor
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pri-mirnas
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single-stranded
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chromatin
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elegans
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helicase
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tumour
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neoplasm
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predisposition
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thyroid
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tumorigenesis
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rna-dependent
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sequence-specific
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stem-loop
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3'utrs
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cystic
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hotspot
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rhabdomyosarcoma
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heterochromatin
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dsrna-binding
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snornas
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retrotransposons
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exoribonuclease
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piwi-interacting
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gene-silencing
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endonucleolytic
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rna-directed
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virus-derived
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mirna-mediated
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multinodular
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overhang
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wilms
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rnai-based
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goiter
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hamartoma
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microrna-mediated
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let-7a
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exportin
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dead-box
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rna-processing
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pre-rrnas
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mirna-based
- 3.1.26.3
- rnai
-
argonaute
- drosophila
-
germline
-
rna-induced
- viruses
- duplex
- ovarian
-
microprocessor
-
pri-mirnas
-
single-stranded
- chromatin
- elegans
- helicase
- tumour
- neoplasm
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predisposition
- thyroid
- tumorigenesis
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rna-dependent
-
sequence-specific
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stem-loop
-
3'utrs
-
cystic
-
hotspot
- rhabdomyosarcoma
- heterochromatin
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dsrna-binding
- snornas
-
retrotransposons
- exoribonuclease
-
piwi-interacting
-
gene-silencing
-
endonucleolytic
-
rna-directed
-
virus-derived
-
mirna-mediated
-
multinodular
-
overhang
-
wilms
-
rnai-based
- goiter
- hamartoma
-
microrna-mediated
-
let-7a
-
exportin
-
dead-box
-
rna-processing
- pre-rrnas
-
mirna-based
Reaction
Endonucleolytic cleavage to a 5'-phosphomonoester =
Synonyms
Aa-RNase III, AbsB, At1g55140, At3g13740, AtRTL1, AtRTL2, AtRTL3, BB_0705, BCG-RNase III, Bm-RNase III, cgR_1959, class 1 RNase III, DCL1, DCL2, DCL3, DCL4, DCR-1, Dicer, Dicer 1, Dicer-1, Dicer-2, Dicer1, double strand-specific endoRNase, Drosha, dsRNA-specific class 1 RNase III-like endoribonuclease, E. coli RNase III, Ec-RNase III, endoribonuclease III, endoribonucleases III, exodeoxyribonuclease III, HCS protein, Hs-Dicer, Hs-Drosha, KREPB10, KREPB9, Lac-RNase III, mini-III, mitochondrial RNA precursor-processing endonuclease 1, More, mRPN1, nuclease, ribo-, D, p241, Pac1p, RBIV RNase III, ribonuclease D, ribonuclease III, ribonuclease III-like protein, ribonuclease type III, RNase D, RNase G, RNase III, RNase III domain A, RNase III double-stranded RNA endonuclease, RNase III endonuclease, RNase III-like protein, RNase O, RNase3, rnc, RNC1, RNC3, RNC4, rncS, RNT1, Rnt1p, Rnt1p RNase III, Sa-RNase III, Sc-Rnt1p, SmRNase III, Tb09.160.3050, Tb927.8.5700, Tm-RNase III, TNase III
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3.1.26.3 ribonuclease IIIAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.1.26.3 - ribonuclease III
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
mraZ mRNA + H2O
?
the degradation of mraZ mRNA is performed by RNase III and the 3'-to-5' exoribonuclease, PNPase. The cleavage site for mraZ mRNA by RNase III is in the coding region
-
-
?
pre-mRNA + H2O
mature mRNA
-
enzyme regulates gene expression by controlling mRNA translation and stability
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
responsible for processing of dsRNA
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
-
responsible for processing and maturation of RNA precursors into functional rRNA, mRNA and other small RNA
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-
?
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
-
-
?
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
-
-
?
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
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
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
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
involved in the production of short interfering RNAs (siRNAs) and for the processing of precursor miRNAs (pre-miRNAs) into microRNAs (miRNAs)
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
responsible for the production of short interfering RNAs and microRNAs that induce gene silencing known as RNA interference
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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the enzyme is able to process rRNAs and to regulate the levels of polynucleotide phosphorylase
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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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
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
processing of precursor dsRNAs into mature microRNAs and small-interfering RNAs
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-
?
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
-
-
?
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
-
-
?
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
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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involved in a variety of cellular functions, including the processing of many non-coding RNAs, mRNA decay, and RNA interference, a dsRNA-binding domain recognizes its substrate by interacting with stems capped with conserved AGNN tetraloops
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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involved in a variety of cellular functions, including the processing of many non-coding RNAs, mRNA decay, and RNA interference, preferred substrate contains NGNN tetraloops
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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enzyme plays multiple roles in the processing of rRNA and mRNA and strongly affects the decay of the sRNA MicA
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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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
-
-
?
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
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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dsRNA-specific endonuclease activity enhances the RNA-silencing suppression activity of another protein (p22) encoded by SPCSV. RNase3 and p22 coexpression reduce siRNA accumulation more efficiently than p22 alone in Nicotiana benthamiana leaves expressing a strong silencing inducer (i.e., dsRNA). RNase3 does not cause intracellular silencing suppression or reduce accumulation of siRNA in the absence of p22 or enhance silencing suppression activity of a protein encoded by a heterologous virus
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-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
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responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
dsRNA + H2O
mature RNA
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reshaping of fully or partially double-stranded RNA precursors in to mature RNAs involved in pre-mRNA splicing, RNA modification, translation, gene silencing, and regulation of developmental timing
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-
?
dsRNA + H2O
mature RNA
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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, enzyme is required for the orderly progression of plant development and for the defense of eukaryotic parasitic DNA and viruses
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-
?
dsRNA + H2O
mature RNA
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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, enzyme is required for the orderly progression of plant development and for the defense of eukaryotic parasitic DNA and viruses
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-
?
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
-
enzyme is involved in the maturation and decay of cellular, phage and plasmid RNAs
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-
?
dsRNA + H2O
mature RNA
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enzyme plays a key role in diverse maturation and degradation processes
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-
?
dsRNA + H2O
mature RNA
-
obligatory step in the maturation and decay of diverse RNAs
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-
?
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
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-
?
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
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-
?
pre-rRNA + H2O
mature rRNA
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enzyme is required for processing
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-
?
pre-snoRNA + H2O
mature snoRNA
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enzyme is required for processing
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?
pre-snRNA + H2O
mature snRNA
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enzyme is required for processing
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-
?
additional information
?
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small hairpins based on the stem structures associated with the Aquifex 16S and 23S rRNA precursors are cleaved at sites that are consistent with production of the immediate precursors to the mature rRNAs. Substrate reactivity is independent of the distal box sequence, but is strongly dependent on the proximal box sequence. RNase III mechanism of dsRNA cleavage, overview
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-
?
additional information
?
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required for 3external transcribed spacer (ETS) cleavage of the pre-rRNA in vivo
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-
?
additional information
?
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mini-III contains an RNase III-like catalytic domain, but curiously lacks the double-stranded RNA binding domain typical of RNase III itself, Dicer, Drosha and other well-known members of this family of enzymes
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-
?
additional information
?
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mini-III contains an RNase III-like catalytic domain, but curiously lacks the double-stranded RNA binding domain typical of RNase III itself, Dicer, Drosha and other well-known members of this family of enzymes
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-
?
additional information
?
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-
Dicer functions as a dsRNA-processing enzyme, producing small interfering RNA (siRNA). Dicer plays important roles in RNA processing, posttranscriptional gene expression control, and defense against virus infection. Bacterial RNase III functions not only as a processing enzyme, but also as a binding protein that binds dsRNA without cleaving it
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-
?
additional information
?
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-
enzyme is essential, and is involved in RNA interference, i.e. RNAi, a post-transcriptional gene-silencing phenomenon, and germ line development
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-
?
additional information
?
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-
In the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs
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-
?
additional information
?
-
-
enzyme is required for maturation of pre-rRNAs
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-
?
additional information
?
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-
enzyme is required for maturation of pre-rRNAs
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-
?
additional information
?
-
-
Dicer-1 and Dicer-2 show different substrate specificity in vivo: Dicer-2 generates small interfering RNAs, siRNAs, from long double-stranded RNA, dsRNA, whereas Dicer-1 produces microRNAs, miRNAs, from pre-miRNA. Dicer-2 can efficiently cleave pre-miRNA in vitro, but phosphate and the Dicer-2 partner protein R2D2 inhibit pre-miRNA cleavage in vivo. Wild-type Dicer-2, but not a mutant defective in ATP hydrolysis, can generate siRNAs faster than it can dissociate from a long dsRNA substrate. Dicer-1 does not efficiently process long dsRNA
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-
?
additional information
?
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-
Drosha recognizes the short internal stem-loop structure of long primary-microRNA transcript as part of a microprocessor complex and cleaves it at the base of the stem-loop, releasing it from the flanking single-stranded regions. Cleavage of both arms of the stem-loop is dependent on the tandem RNase III domains of Drosha binding and cleaving the dsRNA stem. The released stem-loop structure is exported from the nucleus by exportin 5 and is known as a pre-miRNA. Once in the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs. Drosha recognizes and cleaves stem-loop structures within the 50 end of the Dgcr8mRNA inmammalian cells, leading to destabilization of the mRNA. This cleavage therefore serves as amechanism of gene repression, and is proposed to autoregulate the microprocessor complex
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-
?
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
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-
?
additional information
?
-
as a binding protein, RNase III binds and stabilizes certain RNAs, thus suppressing the expression of certain genes
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-
?
additional information
?
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-
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
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-
?
additional information
?
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-
RNase III specifically processes the proU mRNA within a conserved secondary structure extending from position +203 to +293 of the transcript
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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-
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
?
-
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
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?
additional information
?
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the enzyme processes betT and proU mRNA
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?
additional information
?
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processing of dsRNA, the PAZ domain specifically recognizes the 2-nt, 3'-overhangs of a processed dsRNA terminus
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?
additional information
?
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ability of Dicer C-terminus to interact with 5-lipoxygenase
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?
additional information
?
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two-step cleavage of hairpin RNA with 5' overhangs
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?
additional information
?
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two-step cleavage of hairpin RNA with 5' overhangs
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?
additional information
?
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Drosha recognizes the short internal stem-loop structure of long primary-microRNA transcript as part of a microprocessor complex and cleaves it at the base of the stem-loop, releasing it from the flanking single-stranded regions. Cleavage of both arms of the stem-loop is dependent on the tandem RNase III domains of Drosha binding and cleaving the dsRNA stem. The released stem-loop structure is exported from the nucleus by exportin 5 and is known as a pre-miRNA. Once in the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs. Drosha recognizes and cleaves stem-loop structures within the 50 end of the Dgcr8mRNA in mammalian cells, leading to destabilization of the mRNA. This cleavage therefore serves as a mechanism of gene repression, and is proposed to autoregulate the microprocessor complex
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-
?
additional information
?
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processing of dsRNA. Drosha acts on primary transcripts synthesized by RNA polymerase II that typically contain several miRNAs. Site-specific cleavage within irregular, extended hairpin structures (pri-miRNAs) creates the pre-miRNAs that then are delivered by Exportin5 to the cytoplasm for final maturation by Dicer. Drosha functions within a complex termed the microprocessor that contains a protein, DGCR8, that is required for Drosha action
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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-
?
additional information
?
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In the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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Paramecium bursaria Chlorella virus-1
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phylogenetic analysis, enzyme might be important for virus replication
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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enzyme is involved in RNA processing and RNA interference, i.e. RNAi, regulation by a combination of primary and tertiary structural elements allowing a substrate-specific binding and cleavage efficiency
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?
additional information
?
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enzyme is required for maturation of pre-rRNAs
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?
additional information
?
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the enzyme plays an important role in the maturation of a diverse set of RNAs
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?
additional information
?
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the enzyme plays an important role in the maturation of a diverse set of RNAs
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?
additional information
?
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Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its double-stranded RNA binding domains, dsRBD, to recognize a conserved tetraloop fold. The dsRBD adopts the same conformation in both the AAGU and AGAA complexes
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?
additional information
?
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processing of dsRNA, specific bp sequence elements can modulate substrate reactivity, and a network of hydrogen bonds provides an energetically important contribution to Rnt1p binding, a phylogenetic-based substrate alignment analysis reveals a statistically significant exclusion of the UA bp from the position adjacent to the tetraloop. Rnt1p cleaves hairpin structures in pre-rRNAs, pre-mRNAs, and transcripts containing noncoding RNAs such as snoRNAs, as part of the respective maturation pathways. The enzyme also interacts with Gar1p, a protein involved in pseudouridylation reactions, via its C-terminal portion adjacent to the dsRBD
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?
additional information
?
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the enzyme processes ribosomal RNA, small nucleolar RNA, small nuclear RNA, and messenger RNA
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?
additional information
?
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the enzyme Rnt1p binds to RNA stems capped with an NGNN tetraloop, via specific interactions between a structural motif located at the end of the Rnt1p dsRNA-binding domain and the guanine nucleotide in the second position of the loop
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?
additional information
?
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the enzyme Rnt1p binds to RNA stems capped with an NGNN tetraloop, via specific interactions between a structural motif located at the end of the Rnt1p dsRNA-binding domain and the guanine nucleotide in the second position of the loop
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?
additional information
?
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the enzyme Rnt1p binds to RNA stems capped with an NGNN tetraloop, via specific interactions between a structural motif located at the end of the Rnt1p dsRNA-binding domain and the guanine nucleotide in the second position of the loop
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?
additional information
?
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in vitro RNase III is active with MicA when it is in complex with its targets, ompA or lamB mRNAs. MicA is cleaved by RNase III in a coupled way with ompA mRNA
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?
additional information
?
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processing of dsRNA. Pac1p cleaves hairpin structures in pre-rRNAs, pre-mRNAs, and transcripts containing noncoding RNAs such as snoRNAs, as part of the respective maturation pathways
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?
additional information
?
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enzyme SmRNase III is double-strand specific and exhibits different preference for endogenous RNA substrates
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?
additional information
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enzyme SmRNase III is double-strand specific and exhibits different preference for endogenous RNA substrates
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?
additional information
?
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RNAIII and the endoribonuclease III coordinately regulate spa gene expression
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additional information
?
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enzyme RNase III cleavage produces RNA fragments with 5'-phosphate and 3'-hydroxyl termini and a two-nucleotide 3'-overhang. The 5' untranslated region of cspA mRNA is processed by the enzyme. Determination of substrate specificity by sequencing on cDNA libraries generated from RNAs that are co-immunoprecipitated with wild-type RNase III or two different cleavage-defective mutant variants D63A and E135A in vivo, validation of several RNA targets and mapping of cleavage sites of wild-type and mutant enzymes, detailed overview
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?
additional information
?
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enzyme RNase III cleavage produces RNA fragments with 5'-phosphate and 3'-hydroxyl termini and a two-nucleotide 3'-overhang. The 5' untranslated region of cspA mRNA is processed by the enzyme. Determination of substrate specificity by sequencing on cDNA libraries generated from RNAs that are co-immunoprecipitated with wild-type RNase III or two different cleavage-defective mutant variants D63A and E135A in vivo, validation of several RNA targets and mapping of cleavage sites of wild-type and mutant enzymes, detailed overview
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?
additional information
?
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maturation of repeat/spacer-derived short crRNAs by RNase III and the CRISPR-associated Csn1 protein. The co-processed tracrRNA and pre-crRNA carry short 3' overhangs reminiscent of cleavage by the endoribonuclease RNase III
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?
additional information
?
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maturation of repeat/spacer-derived short crRNAs by RNase III and the CRISPR-associated Csn1 protein. The co-processed tracrRNA and pre-crRNA carry short 3' overhangs reminiscent of cleavage by the endoribonuclease RNase III
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?
additional information
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globally regulates the production of antibiotics by Streptomyces coelicolor. Antibiotic production by wild-type and mutant strains of Streptomyces coelicolor analyzed
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additional information
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globally regulates the production of antibiotics by Streptomyces coelicolor. Antibiotic production by wild-type and mutant strains of Streptomyces coelicolor analyzed
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Streptomyces coelicolor absB gene encodes an RNase III family endoribonuclease and is essential for antibiotic biosynthesis. AbsB controls its own expression by sequentially and site specifically cleaving stem-loop segments of its polycistronic transcript
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the gene encoding RNase III in Streptomyces coelicolor is transcribed during exponential phase and is required for antibiotic production and for proper sporulation
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additional information
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globally regulates the production of antibiotics by Streptomyces coelicolor. Antibiotic production by wild-type and mutant strains of Streptomyces coelicolor analyzed
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additional information
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the class 1 enzyme binds and processes small dsRNA molecules, it can cleave long dsRNA molecules, synthetic small interfering RNAs (siRNAs), and plant- and virus-derived siRNAs extracted from sweet potato plants
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endonuclease mRPN1 directly binds with TbRGG2 and exhibits a nuclease-resistant association with two more proteins, 4160 and 8170, it might modulate gRNA utilization by editing complexes
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enzyme is required for maturation of pre-rRNAs
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enzyme is required for maturation of pre-rRNAs
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