Article

 

Monomerization of far-red fluorescent proteins Public Deposited

Downloadable Content

Download PDF
https://ir.library.oregonstate.edu/concern/articles/12579z43s

Descriptions

Attribute NameValues
Creator
Abstract
  • Anthozoa-class red fluorescent proteins (RFPs) are frequently used as biological markers, with far-red (lambda(em) similar to 600-700 nm) emitting variants sought for whole-animal imaging because biological tissues are more permeable to light in this range. A barrier to the use of naturally occurring RFP variants as molecular markers is that all are tetrameric, which is not ideal for cell biological applications. Efforts to engineer monomeric RFPs have typically produced dimmer and blue-shifted variants because the chromophore is sensitive to small structural perturbations. In fact, despite much effort, only four native RFPs have been successfully monomerized, leaving the majority of RFP biodiversity untapped in biomarker development. Here we report the generation of monomeric variants of HcRed and mCardinal, both far-red dimers, and describe a comprehensive methodology for the monomerization of red-shifted oligomeric RFPs. Among the resultant variants is mKelly1 (emission maximum, lambda(em) = 656 nm), which, along with the recently reported mGarnet2 [Matela G, et al. (2017) Chem Commun (Camb) 53: 979982], forms a class of bright, monomeric, far-red FPs.
License
Resource Type
DOI
Date Issued
Journal Title
Journal Volume
  • 115
Rights Statement
Language
ISSN
  • 0027-8424

Relationships

Parents:

This work has no parents.

Items