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

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.

SUBMITTER: Yu D

PROVIDER: S-EPMC4521985 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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

Yu Dan D Baird Michelle A MA Allen John R JR Howe Elizabeth S ES Klassen Matthew P MP Reade Anna A Makhijani Kalpana K Song Yuanquan Y Liu Songmei S Murthy Zehra Z Zhang Shao-Qing SQ Weiner Orion D OD Kornberg Thomas B TB Jan Yuh-Nung YN Davidson Michael W MW Shu Xiaokun X

Nature methods 20150622 8

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. ...[more]

PMID: 26098020

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