Literature summary for 3.1.26.4 extracted from

Kobil, J.H.; Campbell, A.G.
Functional analysis of the domain organization of Trypanosoma brucei RNase HI (2000), Biochem. Biophys. Res. Commun., 270, 336-342.

Search for more literature for 3.1.26.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and N-terminally truncated mutant enzymes as GST-fusion proteins in Escherichia coli temperature sensitive mutant strain MIC3001	Trypanosoma brucei

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of several N-terminally truncated enzyme forms for investigation of structure-function relationship	Trypanosoma brucei

Inhibitors

Inhibitors	Comment	Organism	Structure
Mn2+	can substitute for Mg2+, activates N-terminally truncated mutant RNHIDELTA47 and inhibits the full length enzyme dependent on the presence of the N-terminal 47 amino acids	Trypanosoma brucei

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
nucleus	enzyme contains a nuclear-targeting domain	Trypanosoma brucei	5634	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on, can substitute for Mg2+, activates the full length enzyme dependent on the N-terminal 47 amino acids	Trypanosoma brucei
Mn2+	can substitute for Mg2+, activates N-terminally truncated mutant RNHIDELTA47 and inhibits the full length enzyme dependent on the presence of the N-terminal 47 amino acids	Trypanosoma brucei

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei	-	type I enzyme	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli	Trypanosoma brucei

Reaction

Reaction	Comment	Organism	Reaction ID
Endonucleolytic cleavage to a 5'-phosphomonoester	structure-function relationship, a 42 amino acid noncanonical spacer domain is essential for enzyme function, the nuclear localization domain is not required for function but for RNA binding, it modulates the enzyme manganese-dependent activity	Trypanosoma brucei	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RNA*DNA hybrid + H2O	hydrolyses the RNA strang of the RNA*DNA heteroduplex	Trypanosoma brucei	?	-	?

Subunits

Subunits	Comment	Organism
More	domain organization, the nuclear targeting, which also binds RNA, and the catalytic domains are localized distinctly to the N-terminal and C-terminal parts bound by a spacer domain	Trypanosoma brucei

Synonyms

Synonyms	Comment	Organism
ribonuclease H	-	Trypanosoma brucei
RNase HI	-	Trypanosoma brucei

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Release 2023.1 (January 2023)