Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 62, Issue 9, Pages 1038-1046Publisher
BIRKHAUSER VERLAG AG
DOI: 10.1007/s00018-005-4547-z
Keywords
alternative splicing; G-patch; green-fluorescence protein; RNA splicing; spliceosome; TFIP11; TFIP body; TIP39; TIP39kDa; tuftelin-interacting protein
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Funding
- NIDCR NIH HHS [DE14867, DE13404] Funding Source: Medline
- NIDDK NIH HHS [1 P30 DK48522] Funding Source: Medline
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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.
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