1987
DOI: 10.1002/j.1460-2075.1987.tb02565.x
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The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain.

Abstract: The retroviral oncogene v‐myb encodes a 45,000 Mr nuclear protein (p45v‐myb) that is predominantly associated with the chromatin of transformed cells. It has previously been shown that p45v‐myb, when released from chromatin by salt‐treatment, binds to DNA. To analyse the biochemical properties of p45v‐myb in more detail we have expressed the v‐myb coding region in Escherichia coli. Our results demonstrate that bacterially expressed myb protein has an intrinsic DNA‐binding activity. Using two alternative strate… Show more

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Cited by 159 publications
(113 citation statements)
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“…The motif of WTTEEEFNV is in a single copy starting at amino acid 319. This is similar to that of yeast REB1 (26), a DNA-binding protein that binds rDNA and the promoters of many RNA polymerase II-transcribed genes (27). Therefore, we cannot exclude the possibility that HOS3 binds DNA directly.…”
Section: Discussionmentioning
confidence: 74%
“…The motif of WTTEEEFNV is in a single copy starting at amino acid 319. This is similar to that of yeast REB1 (26), a DNA-binding protein that binds rDNA and the promoters of many RNA polymerase II-transcribed genes (27). Therefore, we cannot exclude the possibility that HOS3 binds DNA directly.…”
Section: Discussionmentioning
confidence: 74%
“…Two of the mutants which neither transformed nor transactivated (mutants 281 and 364) mapped to the highly conserved amino-terminal DNA-binding domain of p48vmyb (21,26 DNA-bound protein, one within the DNA-binding domain itself and one in the less conserved carboxyl terminus of the protein. This suggests a greater complexity for the action of p48v-myb than might be expected from studies of the GAL4 and GCN4 proteins, which appear to contain functionally and physically separable DNA-binding and transcriptional activation domains (for a review, see reference 42).…”
Section: Resultsmentioning
confidence: 99%
“…The 48 kD v-Myb protein is a truncated form of the 75 kD c-Myb protein which in addition to the N-and Cterminal deletions contains 11 amino acid substitutions. Both the c-Myb and the v-Myb proteins are localized in the nucleus (Klempnauer et al, 1984;Boyle et al, 1984), have short half-lives and bind to DNA in a sequence-speci®c fashion (Klempnauer and Sippel, 1987;Biedenkapp et al, 1988).…”
Section: Introductionmentioning
confidence: 99%