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  Regulation of DNA binding activity and nuclear transport of B-Myb in Xenopus oocytes

Humbert-Lan, G., & Pieler, T. (1999). Regulation of DNA binding activity and nuclear transport of B-Myb in Xenopus oocytes. Journal of Biological Chemistry, 274(15), 10293-10300.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-FADB-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DFF3-D
Genre: Journal Article

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Humbert-Lan, G.1, Author              
Pieler, T., Author
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1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: DNA binding activity and nuclear transport of B-Myb in Xenopus oocytes are negatively regulated. Two distinct sequence elements in the carboxy-terminal portion of the protein are responsible for these different inhibitory activities. A carboxy-terminal Xenopus B-Myb protein fragment inhibits the DNA binding activity of the N-terminal repeats in trans, indicating that intramolecular folding may result in masking of the DNA binding function. Xenopus B-Myb contains two separate nuclear localization signals (NLSs), which, in Xenopus oocytes, function only outside the context of the full-length protein. Fusion of an additional NLS to the full-length protein overcomes the inhibition of nuclear import, suggesting that masking of the NLS function rather than cytoplasmic anchoring is responsible for the negative regulation of Xenopus B-Myb nuclear transfer. During Xenopus embryogenesis, when inhibition of nuclear import is relieved, Xenopus B-Myb is preferentially expressed in the developing nervous system and neural crest cells. Within the developing neural tube, Xenopus B-Myb gene transcription occurs preferentially in proliferating, non-differentiated cells.

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 Dates: 2005-08-161999
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: eDoc: 226607
Other: 11472
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 274 (15) Sequence Number: - Start / End Page: 10293 - 10300 Identifier: -