Enzyme-Instructed Assemblies Enable Mitochondria Localization of Histone H2B in Cancer Cells.

ABSTRACT: Presently, little is known of how the inter-organelle crosstalk impacts cancer cells owing to the lack of approaches that can manipulate inter-organelle communication in cancer cells. We found that a negatively charged, enzyme cleavable peptide (MitoFlag) enables the trafficking of histone protein H2B, a nuclear protein, to the mitochondria in cancer cells. MitoFlag interacts with the nuclear location sequence of H2B to block it from entering the nucleus. A protease on the mitochondria cleaves the Flag from the MitoFlag/H2B complex to form assemblies that retain H2B on the mitochondria and facilitate H2B entering the mitochondria. Adding NLS, replacing aspartic acid by glutamic acid residues, or changing the l- to d-aspartic acid residue on MitoFlag abolishes the trafficking of H2B into mi

SUBMITTER: He H 

PROVIDER: S-EPMC7269854 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature