Structural organization and cellular localization of tuftelin-interacting protein 11 (TFIP11).
Cell Mol Life Sci
; 62(9): 1038-46, 2005 May.
Article
em En
| MEDLINE
| ID: mdl-15868102
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Nucleares
/
Processamento Alternativo
/
Proteínas de Transporte Vesicular
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article