Abstract
Tuftelin-interacting protein (TFIP11) was first identified in a yeast two-hybrid screening as a protein interacting with tuftelin. The ubiquitous expression of TFIP11 suggested that it might have other functions in non-dental tissues. TFIP11 contains a G-patch, a protein domain believed to be involved in RNA binding. Using a green fluorescence protein tag, TFIP11 was found to locate in a novel subnuclear structure that we refer to as the TFIP body. An in vivo splicing assay demonstrated that TFIP11 is a novel splicing factor. TFIP11 diffuses from the TFIP body following RNase A treatment, suggesting that the retention of TFIP11 is RNA dependent. RNA polymerase II inhibitor (-amanitin and actinomycin D) treatment causes enlargement in size and decrease in number of TFIP bodies, suggesting that TFIP bodies perform a storage function rather than an active splicing function. The TFIP body may therefore represent a new subnuclear storage compartment for splicing components.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenoviridae / genetics
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Alternative Splicing*
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Amanitins / pharmacology
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Animals
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Cell Line
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Cell Nucleus / drug effects
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Cell Nucleus / metabolism
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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HeLa Cells
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Humans
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Intranuclear Space / drug effects
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Intranuclear Space / metabolism
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Mice
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Microscopy, Confocal
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Microscopy, Fluorescence
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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RNA Polymerase II / antagonists & inhibitors
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RNA Splicing Factors
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Ribonuclease, Pancreatic / metabolism
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Transfection
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Vesicular Transport Proteins / genetics
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Vesicular Transport Proteins / metabolism*
Substances
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Amanitins
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Nuclear Proteins
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RNA Splicing Factors
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Recombinant Fusion Proteins
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TFIP11 protein, human
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Vesicular Transport Proteins
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Green Fluorescent Proteins
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RNA Polymerase II
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Ribonuclease, Pancreatic