A Rapid and Simple Method of Evaluating the Dimeric Tendency of Fluorescent Proteins in Living Cells Using a Truncated Protein of Importin α as Fusion Tag

Enhanced green fluorescent protein (EGFP) and its yellow variant (Venus) are weakly dimeric under physiological conditions. We designed a simple method to evaluate the dimeric tendency of fluorescent proteins in living mammalian cells. A novel single mutation, A206L, interfering with the hydrophobic...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2012, Vol.76 (2), p.388-390
Main Authors: NAKAGAWA, Chika, NISHIMURA, Shigenori, SENDA-MURATA, Kaori, SUGIMOTO, Kenji
Format: Article
Language:English
Subjects:
alpha Karyopherins - genetics
Animals
Biological and medical sciences
Cells - chemistry
Cytological Techniques - methods
fluorescent protein (FP)
Fundamental and applied biological sciences. Psychology
Green Fluorescent Proteins
Hydrophobic and Hydrophilic Interactions
importin alpha (importin α)
Luminescent Proteins
Methods
Mutation, Missense
nuclear-pore complex (NPC)
Protein Multimerization
Recombinant Fusion Proteins
Venus
weak dimer
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Summary:Enhanced green fluorescent protein (EGFP) and its yellow variant (Venus) are weakly dimeric under physiological conditions. We designed a simple method to evaluate the dimeric tendency of fluorescent proteins in living mammalian cells. A novel single mutation, A206L, interfering with the hydrophobic interactions of the dimer interface in Venus, contributed to its monomerization, and was as effective as the A206K mutation in this assay.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.110677