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ID: 226607.0, MPI für biophysikalische Chemie / Molekulare Biologie (Dr. Thomas M. Jovin)
Regulation of DNA binding activity and nuclear transport of B-Myb in Xenopus oocytes
Authors:Humbert-Lan, G.; Pieler, T.
Language:English
Date of Publication (YYYY-MM-DD):1999
Title of Journal:Journal of Biological Chemistry
Volume:274
Issue / Number:15
Start Page:10293
End Page:10300
Copyright:Jahrbuch 2000, Copyright MPG 2000
Review Status:Peer-review
Audience:Not Specified
Intended Educational Use:No
Abstract / Description: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.
Last Change of the Resource (YYYY-MM-DD):2005-08-16
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
External Affiliations:Institut für Biochemie und Molekulare Zellbiologie der Universität Göttingen, Humboldtallee 23, 37073 Göttingen, Germany
Identifiers:LOCALID:11472
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