کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2833592 | 1163882 | 2006 | 12 صفحه PDF | دانلود رایگان |

CArG box-binding factor-A (CBF-A) interacts with the penta-decamer (pd) element that is a conserved sequence element within mouse Vκ promoters. The pd element acts in synergy with the octamer element to stimulate κ 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.
Journal: Molecular Immunology - Volume 43, Issue 6, February 2006, Pages 690–701