Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-06

AUTHORS

N P Mahajan, K Linder, G Berry, G W Gordon, R Heim, B Herman

ABSTRACT

It has been hypothesized that interaction of Bcl-2 and Bax may regulate apoptosis. The spatial and temporal interaction of Bcl-2 and Bax at the single cell level has not, however, been demonstrated. To achieve this goal, we have developed two-fusion FRET (fluorescence resonance energy transfer). Using green fluorescent protein (GFP)-Bax and blue fluorescent protein (BFP)-Bcl-2 fusion proteins coexpressed in the same cell, we demonstrate a direct interaction between Bcl-2 and Bax in individual mitochondria. Mitochondrially localized cytochrome c-GFP and BFP-Bcl-2 showed little or no FRET, while nuclear-localized GFP-human papillomavirus E6 and BFP-Bcl-2 did not interact when coexpressed in the same cell. These findings indicate that two-fusion FRET provides an opportunity to examine the interaction between two different proteins coexpressed in single intact mammalian cells. More... »

PAGES

547-552

Journal

TITLE

Nature Biotechnology

ISSUE

6

VOLUME

16

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt0698-547

    DOI

    http://dx.doi.org/10.1038/nbt0698-547

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1013031729

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9624685


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