A naturally-monomeric infrared fluorescent protein for protein labeling in vivo

Infrared fluorescent proteins (IFPs) provide an additional color to GFP and its red homologs in protein labeling. Based on structural analysis of the dimer interface, a monomeric bateriophytochrome is identified from a sequence database, and is engineered into a naturally-monomeric IFP (mIFP). We de...

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Detalles Bibliográficos
Autores principales: Yu, Dan, Baird, Michelle A., Allen, John R., Howe, Elizabeth S., Klassen, Matthew P., Reade, Anna, Makhijani, Kalpana, Song, Yuanquan, Liu, Songmei, Murthy, Zehra, Zhang, Shao-Qing, Weiner, Orion D., Kornberg, Thomas B., Jan, Yuh-Nung, Davidson, Michael W., Shu, Xiaokun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521985/
https://www.ncbi.nlm.nih.gov/pubmed/26098020
http://dx.doi.org/10.1038/nmeth.3447
Descripción
Sumario:Infrared fluorescent proteins (IFPs) provide an additional color to GFP and its red homologs in protein labeling. Based on structural analysis of the dimer interface, a monomeric bateriophytochrome is identified from a sequence database, and is engineered into a naturally-monomeric IFP (mIFP). We demonstrate that mIFP correctly labels proteins in live Drosophila and zebrafish requiring no exogenous cofactor, and will thus be useful in molecular, cell and developmental biology.

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