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The kappa promoter penta-decamer binding protein CBF-A interacts specifically with nucleophosmin in the nucleus only.
Aranburu, Alaitz; Bennett, Matthew; Leanderson, Tomas.
Afiliação
  • Aranburu A; Inflammation and Immunology Unit, BMC I:13, Department of Experimental Medical Science, Lund University, 221 84 Lund, Sweden.
Mol Immunol ; 43(6): 690-701, 2006 Feb.
Article em En | MEDLINE | ID: mdl-16360014
CArG box-binding factor-A (CBF-A) interacts with the penta-decamer (pd) element that is a conserved sequence element within mouse Vkappa promoters. The pd element acts in synergy with the octamer element to stimulate kappa transcription, especially in later stages of B cell development. To get further insight in the mechanism for CBF-A action we have characterised its protein-protein interactions. We show here that CBF-A interacts specifically with nucleophosmin (NPM). This interaction occurs via the homo-oligomerisation domain of NPM and the N-terminus of CBF-A and was exclusive for the nuclear compartment while the two proteins failed to interact in the cytosol. In contrast, CBF-A formed homocomplexes in this compartment. CBF-A was also shown to localise to the nucleoli, most likely dependent on a functional interaction with NPM. Lastly, the sequence fine specificity of CBF-A complexes in the nucleus and cytoplasm were found to differ and nuclear protein-DNA complexes were shown to contain NPM. Thus, CBF-A participates in several protein-protein interactions that may modulate its subcellular localisation and target gene specificity.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Limite: Animals / Humans Idioma: En Ano de publicação: 2006 Tipo de documento: Article
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Limite: Animals / Humans Idioma: En Ano de publicação: 2006 Tipo de documento: Article