Literature summary for 3.1.26.5 extracted from

Reiner, R.; Alfiya-Mor, N.; Berrebi-Demma, M.; Wesolowski, D.; Altman, S.; Jarrous, N.
RNA binding properties of conserved protein subunits of human RNase P (2011), Nucleic Acids Res., 39, 5704-5714.

Search for more literature for 3.1.26.5

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 in Escherichia coli	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
nucleus	-	Homo sapiens	5634	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 from Escherichia coli as soluble and refolded proteins	Homo sapiens

Synonyms

Synonyms	Comment	Organism
RNase P	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Homo sapiens

General Information

General Information	Comment	Organism
additional information	the catalytic RNP has an H1 RNA moiety associated with ten distinct protein subunits. Five out of eight of these protein subunits, Rpp20, Rpp21, Rpp25, Rpp29, and Pop5, prepared in refolded recombinant forms, bind to H1 RNA in vitro. Rpp20 and Rpp25 bind jointly to H1 RNA, even though each protein can interact independently with this transcript. Nuclease footprinting analysis reveals that Rpp20 and Rpp25 recognize overlapping regions in the P2 and P3 domains of H1 RNA. Rpp21 and Rpp29, which are sufficient for reconstitution of the endonucleolytic activity, bind to separate regions in the catalytic domain of H1 RNA, subunit binding site analysis on H1 RNA, overview	Homo sapiens
physiological function	nuclear RNase P is required for transcription and processing of tRNA	Homo sapiens

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Release 2023.1 (January 2023)