Nuclear Compartmentalization of the v-<i>myb</i> Oncogene Product

Boyle, W J; Lampert, Martha A.; Li, A C; Baluda, M A

doi:10.1128/mcb.5.11.3017-3023.1985

Molecular and Cellular Biology

1985

DOI: 10.1128/mcb.5.11.3017-3023.1985

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Nuclear Compartmentalization of the v-myb Oncogene Product

W J Boyle¹,

Martha A. Lampert²,

A C Li

et al.

Abstract: Nuclei obtained from chicken leukemic myeloblasts transformed by avian myeloblastosis virus were fractionated into various subnuclear compartments, which were then analyzed by specific immunoprecipitation for the presence of the leukemogenic product, p48v-myb, of the viral oncogene. In cells labeled for 30 or 60 min with L-[35S]methionine and in unlabeled exponentially dividing leukemic cells analyzed by Western blotting, p48v-myb was detected within the nucleoplasm (29 +/- 9% [standard deviation] of the total… Show more

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1986

1988

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Cited by 18 publications

References 48 publications

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Identification and characterization of the protein encoded by the human c-myb proto-oncogene.

Klempnauer¹,

Bonifer²,

Sippel³

1986

The EMBO Journal

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We have identified the product of the human c‐myb proto‐oncogene as a 80,000‐Mr protein, p80c‐myb, by using polyclonal and monoclonal antibodies raised against a bacterially synthesized polypeptide from the amino terminus of the viral myb protein. p80c‐myb shares at least two distinct antigenic sites with the amino terminal region of the v‐myb protein. p80c‐myb is found only in hematopoietic cells or in cells that contain amplified c‐myb genes. Like the chicken myb proteins, p80c‐myb is a nuclear DNA‐binding protein that is predominantly associated with chromatin and exhibits a short half‐life of approximately 1 hour.

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Identification and characterization of the protein encoded by the human c-myb proto-oncogene.

Klempnauer¹,

Bonifer²,

Sippel³

1986

The EMBO Journal

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show abstract

The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain.

1987

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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 strategies, (i) inhibition of DNA‐binding by monoclonal antibodies and (ii) analysis of DNA‐binding activities of partially deleted forms of the bacterial myb protein, we show that the DNA‐binding domain is located in the amino‐terminal region of the v‐myb protein. This region has been highly conserved between myb genes of different species. Our results are therefore consistent with the hypothesis that DNA‐binding is an important aspect of myb protein function.

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Rapid turnover of adenovirus E1A is determined through a co-translational mechanism that requires an aminoterminal domain.

1988

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The product of the adenovirus E1A 13S mRNA can both stimulate and repress the expression of certain viral and cellular genes. As with several other regulatory proteins, E1A has a short half‐life, approximately 40 min. Although this short half‐life is observed in cells expressing the E1A gene, it is not the case with cells injected with E1A protein, where its half‐life is very long, generally greater than 15 h. We have sought to reconcile these apparent differences in E1A stability. Using Xenopus oocytes, we find that E1A exhibits its characteristic short half‐life when it is synthesized from injected mRNA while it has a very long half‐life when it is injected as a protein synthesized originally in Escherichia coli or reticulocyte lysates. In order to delineate the amino acids responsible for rapid E1A turnover, several deletion mRNAs were constructed, injected into oocytes, and E1A half‐life determined. Carboxyl‐terminal deletions and an internal deletion of residues 38‐86 failed to increase the half‐life of E1A. In contrast, amino‐terminal deletions of 70 and 14 residues resulted in very stable E1A proteins (t1/2 greater than 20 h). Furthermore, deletion of the second amino acid, an arginine, resulted in a stable E1A protein. The amino‐terminal region of E1A was able to induce the rapid turnover of a normally stable protein, beta‐globin, in oocytes injected with an E1A‐globin chimeric mRNA. This E1A‐induced instability of globin was abolished, however, when the protein was first synthesized in reticulocyte lysates and then injected into oocytes. The amino‐terminal region of E1A is also important in governing halflife in adenovirus‐infected HeLa cells. These results demonstrate that the half‐life of E1A is established cotranslationally through a mechanism involving sequences within the amino‐terminal 37 residues.

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Nuclear Compartmentalization of the v-myb Oncogene Product

Cited by 18 publications

References 48 publications

Identification and characterization of the protein encoded by the human c-myb proto-oncogene.

Identification and characterization of the protein encoded by the human c-myb proto-oncogene.

The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain.

Rapid turnover of adenovirus E1A is determined through a co-translational mechanism that requires an aminoterminal domain.

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