Different mCherry isoforms show distinct photophysical properties in FRET tandem constructs.

ABSTRACT: Fluorescent proteins are important reporter tools to investigate biological processes in the cellular environment at the molecular level. The spectrum of available fluorescent proteins has been greatly expanded by red-emitting fluorescent variants such as the commonly used mCherry. However, the presence of alternative translation initiation sites (aTIS) in mCherry allows for production of shorter protein isoforms with different properties that can bias the results of studies in which mCherry intensities are evaluated. In the present study, we used a novel approach of spectroscopic techniques, including Förster resonance energy transfer (FRET) to investigate the impact of aTIS on the photophysical properties and the functionality of mCherry in both, prokaryotic and eukaryotic expression sys

SUBMITTER: Hoffmann B 

PROVIDER: S-EPMC12708940 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature