PUBLICATION

A naturally monomeric infrared fluorescent protein for protein labeling in vivo

Authors
Yu, D., Baird, M.A., Allen, J.R., Howe, E.S., Klassen, M.P., Reade, A., Makhijani, K., Song, Y., Liu, S., Murthy, Z., Zhang, S.Q., Weiner, O.D., Kornberg, T.B., Jan, Y.N., Davidson, M.W., Shu, X.
ID
ZDB-PUB-150623-3
Date
2015
Source
Nature Methods   12(8): 763-5 (Journal)
Registered Authors
Reade, Anna
Keywords
Fluorescence imaging, Fluorescent proteins, Cellular imaging, Transgenic organisms
MeSH Terms
  • Drosophila melanogaster
  • Mutation
  • Zebrafish
  • Protein Conformation
  • HeLa Cells
  • Humans
  • Animals
  • Transfection
  • Plasmids/metabolism
  • Recombinant Fusion Proteins/chemistry
  • Green Fluorescent Proteins/chemistry*
  • Animals, Genetically Modified
  • Mice
  • Histidine/chemistry
  • Neurons/metabolism
  • Luminescent Proteins/chemistry
  • Infrared Rays*
  • Molecular Sequence Data
  • Protein Multimerization
  • Fluorescent Dyes/chemistry
  • Amino Acid Sequence
  • DNA/chemistry
  • Developmental Biology
PubMed
26098020 Full text @ Nat. Methods
Abstract
Infrared fluorescent proteins (IFPs) provide an additional color to GFP and its homologs in protein labeling. Drawing on structural analysis of the dimer interface, we identified a bacteriophytochrome in the sequence database that is monomeric in truncated form and engineered it into a naturally monomeric IFP (mIFP). We demonstrate that mIFP correctly labels proteins in live cells, Drosophila and zebrafish. It should be useful in molecular, cell and developmental biology.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping