ArticleFEBS open bio2016
In vivo fluorescence correlation spectroscopy analyses of FMBP-1, a silkworm transcription factor.
Article in FEBS open bio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Understanding and manipulating extracellular behaviors of Wnt ligands.In vitro cellular & developmental biology. Animal · 2024Review
- Cell cycle-dependent binding between Cyclin B1 and Cdk1 revealed by time-resolved fluorescence correlation spectroscopy.Open biology · 2022Article
- New insights into the proteins interacting with the promoters of silkworm fibroin genes.Scientific reports · 2021Article
- Article
- Insights into the regulatory characteristics of silkworm fibroin gene promoters using a modified Gal4/UAS system.Transgenic research · 2019Article
- Measuring Mobility in Chromatin by Intensity-Sorted FCS.Biophysical journal · 2019Article
- Control of Hox transcription factor concentration and cell-to-cell variability by an auto-regulatory switch.Development (Cambridge, England) · 2019Article
- Mapping the Dynamics of the Glucocorticoid Receptor within the Nuclear Landscape.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroin modulator-binding protein 1 (FMBP-1) is a silkworm transcription factor that has a unique DNA-binding domain called the one score and three amino acid peptide repeat (STPR). Here we used fluorescence correlation spectroscopy (FCS) to analyze the diffusion properties of an enhanced green fluorescent protein-tagged FMBP-1 protein (EGFP-FMBP-1) expressed in posterior silk gland (PSG) cells of Bombyx mori at the same developmental stage as natural FMBP-1 expression. EGFP-FMBP-1 clearly localized to cell nuclei. From the FCS analyses, we identified an immobile DNA-bound component and three discernible diffusion components. We also used FCS to observe the movements of wild-type and mutant EGFP-FMBP-1 proteins in HeLa cells, a simpler experimental system. Based on previous in vitro observation, we also introduced a single amino acid substitution in order to suppress stable FMBP-1-DNA binding; specifically, we replaced the ninth Arg in the third repeat within the STPR domain with Ala. This mutation completely disrupted the slowest diffusion component as well as the immobile component. The diffusion properties of other FMBP-1 mutants (e.g. mutants with N-terminal or C-terminal truncations) were also analyzed. Based on our observations, we suggest that the four identifiable movements might correspond to four distinct FMBP-1 states: (a) diffusion of free protein, (b) and
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