Format

Send to

Choose Destination
Nat Commun. 2019 Mar 12;10(1):1179. doi: 10.1038/s41467-019-09088-y.

Quantifying protein dynamics and stability in a living organism.

Author information

1
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
2
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA. mgruebel@illinois.edu.
3
Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA. mgruebel@illinois.edu.
4
Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA. mgruebel@illinois.edu.
5
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA. cmmdavis@illinois.edu.
6
Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA. cmmdavis@illinois.edu.

Abstract

As an integral part of modern cell biology, fluorescence microscopy enables quantification of the stability and dynamics of fluorescence-labeled biomolecules inside cultured cells. However, obtaining time-resolved data from individual cells within a live vertebrate organism remains challenging. Here we demonstrate a customized pipeline that integrates meganuclease-mediated mosaic transformation with fluorescence-detected temperature-jump microscopy to probe dynamics and stability of endogenously expressed proteins in different tissues of living multicellular organisms.

PMID:
30862837
PMCID:
PMC6414637
DOI:
10.1038/s41467-019-09088-y
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center