Literature summary for 3.1.26.11 extracted from

Ma, M.; Li de la Sierra-Gallay, I.; Lazar, N.; Pellegrini, O.; Lepault, J.; Condon, C.; Durand, D.; van Tilbeurgh, H.
Trz1, the long form RNase Z from yeast, forms a stable heterohexamer with endonuclease Nuc1 and mutarotase (2017), Biochem. J., 474, 3599-3613 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli BL21 Gold (DE3)	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P36159	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharomyces cerevisiae

Subunits

Subunits	Comment	Organism
More	Trz1, Nuc1 and mutarotase form a very stable heterohexamer, composed of two copies of each of the three subunits. A Nuc1 homodimer is at the center of the complex, creating a two-fold symmetry and interacting with both Trz1 and mutarotase. Enzymatic characterization of the ternary complex revealed that the activities of Trz1 and mutarotase are not affected by complex formation, but that the Nuc1 activity is completely inhibited by mutarotase and partially by Trz1. This suggests that mutarotase and Trz1 might be regulators of the Nuc1 apoptotic nuclease activity	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
TRZ1	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)