3.1.26.12: ribonuclease E
This is an abbreviated version!
For detailed information about ribonuclease E, go to the full flat file.
Word Map on EC 3.1.26.12
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3.1.26.12
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degradosome
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polynucleotide
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phosphorylase
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pnpase
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srnas
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endonuclease
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hfq
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helicase
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endonucleolytic
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exoribonuclease
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single-stranded
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enolase
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stem-loops
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polya
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rna-binding
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polycistronic
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ribonucleolytic
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e-dependent
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base-pairing
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dead-box
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autoregulation
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e-mediated
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e-like
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ompa
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endoribonucleolytic
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5'-terminal
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intercistronic
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cole1-type
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monophosphorylated
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5'-monophosphorylated
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shine-dalgarno
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rho-independent
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hfq-dependent
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glucosamine-6-phosphate
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riboswitches
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au-rich
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glm
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rna-processing
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crescentus
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analysis
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medicine
- 3.1.26.12
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degradosome
- polynucleotide
- phosphorylase
- pnpase
- srnas
- endonuclease
- hfq
- helicase
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endonucleolytic
- exoribonuclease
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single-stranded
- enolase
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stem-loops
- polya
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rna-binding
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polycistronic
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ribonucleolytic
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e-dependent
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base-pairing
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dead-box
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autoregulation
-
e-mediated
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e-like
- ompa
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endoribonucleolytic
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5'-terminal
-
intercistronic
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cole1-type
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monophosphorylated
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5'-monophosphorylated
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shine-dalgarno
-
rho-independent
-
hfq-dependent
- glucosamine-6-phosphate
- riboswitches
-
au-rich
- glm
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rna-processing
- crescentus
- analysis
- medicine
Reaction
endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions =
Synonyms
Ams/Rne/Hmp1 polypeptide, AqaRng, endoribonuclease E, endoribonuclease RNase E, More, NCgl2281, ribonuclease E, RNase E, RNase E/G, RNase E/G-type endoribonuclease, RNase ES, RNase EV, RNaseE, Rne, Rne protein, RneC, Rng, SSO1404, SynRne
ECTree
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Subunits
Subunits on EC 3.1.26.12 - ribonuclease E
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dimer
oligomer
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x * 115000, about, sequence calculation, x * 150000-160000, SDS-PAGE
tetramer
additional information
tetramer
dimer composed of two dimers, tertiary and quarternary structure, overview
tetramer
a pair of dimers, the quaternary organization of RNase E is flexible, modelling, apoprotein formation leads to a conformational change in which the 5' sensor and S1 subdomains move as a single unit through an angle between the apoprotein and holoprotein state, overview
tetramer
the catalytic domain of RNase E forms a homotetramer with a molecular mass of roughly 260 kDa
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catalytic domain structure, homology-based modelling, overview
additional information
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RNase E forms a degradosome complex together with RhlB, the metabolic enzyme aconitase, PNPase, and the exoribonuclease RNase D
additional information
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N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity
additional information
structural characterization of the RNase E S1 domain, residues 25-125, by NMR, and identification of its oligonucleotide-binding and dimerization interfaces, overview, isolated S1 domain, which shows an OB fold, undergoes a specific monomer-dimer equilibrium in solution with a KD in the millimolar range
additional information
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structural characterization of the RNase E S1 domain, residues 25-125, by NMR, and identification of its oligonucleotide-binding and dimerization interfaces, overview, isolated S1 domain, which shows an OB fold, undergoes a specific monomer-dimer equilibrium in solution with a KD in the millimolar range
additional information
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the enzyme is localized in a multi-protein complex, the RNA degradosome
additional information
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the enzyme is localized in a multi-protein complex, the RNA degradosome, RNase E S1 catalytic domain structure analysis, structure-function relationship, 4 catalytic domains associate in an interwoven quarternary structure, the catalytic domain structure is structurally congruent to a deoxyribonuclease, the N-terminal half harbors the catalytic domain, while the C-terminal half is involved in interaction with the other protein components of the degradosome, i.e. RNA helicase, enolase, and PNPase
additional information
the enzyme is localized in a multi-protein complex, the RNA degradosome, RNase E S1 catalytic domain structure analysis, structure-function relationship, 4 catalytic domains associate in an interwoven quarternary structure, the catalytic domain structure is structurally congruent to a deoxyribonuclease, the N-terminal half harbors the catalytic domain, while the C-terminal half is involved in interaction with the other protein components of the degradosome, i.e. RNA helicase, enolase, and PNPase
additional information
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the enzyme is part of the RNA degradosome, a large multiprotein machine to process and degrade RNA, organization, overview, the enzymes' C-terminal half contains the binding sites for the three other degradosome protein components DEAD-box RNA helicase RhlB, enolase, and polynucleotide phosphorylase PNPase, the C-terminal half of RNase E acts as a scaffold upon which the other components of the complex are assembled, functional analysis of enzyme domains by using deletion mutants of RNase E, overview
additional information
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the enzyme needs to be in a multimeric state for activation by 5' monophosphorylated RNA substrates, possible multimerization mechanism dependent on 5' activation, overview
additional information
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the enzymes' conserved N-terminal catalytic domain forms homotetramers binding up to four molecules of specific RNA substrate, the tetramers forms a D2 dihedral symmetry, X-ray scattering, analytical ultracentrifugation, mass spectrometry, and circular dichroism used for structure analysis, overview
additional information
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the N-terminal region N-Rne contains the catalytic domain
additional information
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the Rne protein is composed of an N-terminal catalytic domain, two proline-rich segments, an arginine-rich RNA-binding site ARRBS segment, and a proline-rich and acidic domain, domain organization, overview
additional information
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three-dimensional enzyme structure with an essential N-terminal RNase E domain of the S1 family RNA-binding domain fold, the residues involved in cell growth and feedback regulation of RNase E synthesis form two cluster, e.g. Phe57, Phe67, and Tyr112, or Lys37 and Tyr60, overview, structural modeling of the S1 domain
additional information
RNase E is divided into domains of defined function and structure, the tetramer has two nonequivalent subunit interfaces, one of which is mediated by a single, tetrathiol-zinc complex, which we refer to as a Zn-link motif. One or both interfaces organize the active site, which is distinct from the primary site of RNA binding
additional information
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RNase E is divided into domains of defined function and structure, the tetramer has two nonequivalent subunit interfaces, one of which is mediated by a single, tetrathiol-zinc complex, which we refer to as a Zn-link motif. One or both interfaces organize the active site, which is distinct from the primary site of RNA binding
additional information
RNase E forms a degradosome assembly in which the canonical components associated with the CTD are a DEAD-box RNA helicase (RhlB), the glycolytic enzyme enolase, and the exoribonuclease PNPase
additional information
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N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity
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additional information
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the enzyme is localized in a multi-protein complex, the RNA degradosome
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additional information
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the catalytic site is located at the N-terminus, residues 1-413
additional information
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RNase E forms a degradosome assembly in which the canonical components associated with the CTD are a DEAD-box RNA helicase (RhlB), the glycolytic enzyme enolase, and the exoribonuclease PNPase
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additional information
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the catalytic site is located at the N-terminus, residues 1-406