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Reference: Mizumura H, et al. (1999) Stable association of 70-kDa heat shock protein induces latent multisite specificity of a unisite-specific endonuclease in yeast mitochondria. J Biol Chem 274(36):25682-90

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Abstract

The multisite-specific endonuclease Endo.SceI of yeast mitochondria is unique among endonucleases because its 50-kDa subunit forms a stable dimer with the mitochondrial 70-kDa heat shock protein (mtHSP70), which otherwise fulfills a chaperone function by binding transiently to unfolded proteins. Here we show that the mtHSP70 subunit confers broader sequence specificity, greater stability, and higher activity on the 50-kDa subunit. The 50-kDa subunit alone displayed weaker activity and highly sequence-specific endonuclease activity. The 50-kDa protein exists as a heterodimer with mtHSP70 in vivo, allowing Endo.SceI to cleave specifically at multiple sites on mitochondrial DNA. Endo.SceI may have evolved from a highly specific endonuclease that gained broader sequence specificity after becoming a stable partner of mtHSP70.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Mizumura H, Shibata T, Morishima N
Primary Lit For
SSC1 | ENS2 | Endonuclease SceI

Gene Ontology Annotations 1 entry for 1 gene

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Gene/ComplexQualifierGene Ontology TermAnnotation ExtensionEvidenceSourceAssigned On
SSC1enablesenzyme regulator activityIDASGD2013-08-07
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