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.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Animals, Genetically Modified
-
DNA / chemistry
-
Developmental Biology
-
Drosophila melanogaster
-
Fluorescent Dyes / chemistry
-
Green Fluorescent Proteins / chemistry*
-
HeLa Cells
-
Histidine / chemistry
-
Humans
-
Infrared Rays*
-
Luminescent Proteins / chemistry
-
Mice
-
Molecular Sequence Data
-
Mutation
-
Neurons / metabolism
-
Plasmids / metabolism
-
Protein Conformation
-
Protein Multimerization
-
Recombinant Fusion Proteins / chemistry
-
Transfection
-
Zebrafish
Substances
-
Fluorescent Dyes
-
Luminescent Proteins
-
Recombinant Fusion Proteins
-
Green Fluorescent Proteins
-
polyhistidine
-
Histidine
-
DNA