Literature summary for 3.1.26.5 extracted from

Li, D.; Meyer, M.H.; Willkomm, D.K.; Keusgen, M.; Hartmann, R.K.
Analysis of bacterial RNase P RNA and protein interaction by a magnetic biosensor technique (2010), Biochimie, 92, 772-778.

Search for more literature for 3.1.26.5

Application

Application	Comment	Organism
additional information	magnetic sensor technique suitable for the measurement of specific RNA-protein interactions, whereby properties of the streptavidin-coated magnetic beads decide on success or failure of the technique	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
protein overexpressed in Escherichia coli with an N-terminal hexahistidyl tag, RNA subunit produced by run-off in vitro T7 transcription from plasmid pDW98 linearized with BsaAI	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	assay buffer	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by Ni-NTA affinity chromatography	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	interaction of immobilized RNase P protein and 3'-biotinylated RNase P RNA bound to streptavidin-coated magnetic beads. The protein binds to the C-domain of P RNA in the P2-J2/3-P3-J3/4-P4-J18/2 region. Kd values of about 1-2 nanomol (at 4.5 mM Mg2+ and 150 mM NH4+) for RNase P RNA and protein. A bacterial-like 1-bp insertion and 2-nt deletion in the helix P2/P3 region largely improves affinity, thus these elements are crucial for interaction of the two RNase P subunits	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
ribonuclease P	-	Escherichia coli
RNase P	-	Escherichia coli

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Release 2023.1 (January 2023)