ISBN: 9783842882911

The oncogene v-myb of the retroviruses AMV (avian myeloblastosis virus) and E26 (avian leukaemia virus) encodes a transcription factor (v-Myb) which is a truncated homolog of its cellular… Mehr…

The oncogene v-myb of the retroviruses AMV (avian myeloblastosis virus) and E26 (avian leukaemia virus) encodes a transcription factor (v-Myb) which is a truncated homolog of its cellular progenitor c-Myb. c-Myb plays an essential role in the development of haematopoietic cells and is known to be a regulator for many target genes. v-Myb AMV is responsible for the transformation of myelomonocytic cells and for arresting them in an immature stage, presumably because of a deregulation of the expression of specific target genes. In addition to the truncation of the coding region, a number of amino acid substitutions are responsible for the high oncogenicity of v-Myb AMV. Due to the amino acid substitutions, v-Myb AMV and v-Myb E26 differ in their target gene spectrum. The chicken mim-1 gene is activated by v-Myb E26 and c-Myb but not by v-Myb AMV. The gene consists of two cis-regulatory regions, a Myb responsive promoter and a cell-specific Myb-inducible enhancer. Recently, it has been proven that two amino acid substitutions in a hydrophobic patch in the transactivation domain of v-Myb AMV are sufficient to disrupt its ability to stimulate the enhancer. This work focuses on the consequences of these amino acid substitutions by investigating protein-protein interactions of the hydrophobic region of v-Myb AMV in comparison to v Myb E26. Previous experiments identified GRP78 as an interaction partner of v Myb. In this study, a cytosolic variant of GRP78, GRP78va, was confirmed to interact with both v-Myb proteins. It was shown that its interaction site is limited to a very small region of v-Myb preceding the hydrophobic patch. Additionally, it was shown that GRP78va associated with all other members of the Myb-family and also with C/EBPss and HIPK2, suggesting a non-sequence-specific binding of GRP78va. Furthermore, reporter gene experiments demonstrated a repressing effect of GRP78va on the transactivation potential of v-Myb E26. In addition, GST pull down assays and co-immunoprecipitation experiments were used to precipitate endogenous proteins that could represent potential interaction partners of v-Myb. SDS-PAGE analysis revealed candidate bands, but mass spectrometry analysis failed to identify any proteins relevant for interaction with v Myb. Two other proteins were tested for their interaction with the hydrophobic patch of v-Myb. Co-immunoprecipitation experiments confirmed that C/EBPss interacts with the hydrophobic region of v-Myb and that the amino acid substitutions seem to affect the interaction in a negative way. Furthermore, PRMT4 was identified as an interaction partner of v-Myb. Mapping experiments showed the interaction to be mediated by the hydrophobic region. The point mutations in v-Myb AMV appear to positively influence the affinity for PRMT4. The fact that a SUMO binding motif is located in the same region might suggest a potential involvement of SUMO in the interaction of PRMT4 and v-Myb. Bücher > Fremdsprachige Bücher > Englische Bücher 22.0 cm x 15.5 cm x 0.8 cm mm , Diplomica Verlag, Taschenbuch, Diplomica Verlag<

ISBN: 9783842882911

The oncogene v-myb of the retroviruses AMV (avian myeloblastosis virus) and E26 (avian leukaemia virus) encodes a transcription factor (v-Myb) which is a truncated homolog of its cellular… Mehr…

The oncogene v-myb of the retroviruses AMV (avian myeloblastosis virus) and E26 (avian leukaemia virus) encodes a transcription factor (v-Myb) which is a truncated homolog of its cellular progenitor c-Myb. c-Myb plays an essential role in the development of haematopoietic cells and is known to be a regulator for many target genes. v-Myb AMV is responsible for the transformation of myelomonocytic cells and for arresting them in an immature stage, presumably because of a deregulation of the expression of specific target genes. In addition to the truncation of the coding region, a number of amino acid substitutions are responsible for the high oncogenicity of v-Myb AMV. Due to the amino acid substitutions, v-Myb AMV and v-Myb E26 differ in their target gene spectrum. The chicken mim-1 gene is activated by v-Myb E26 and c-Myb but not by v-Myb AMV. The gene consists of two cis-regulatory regions, a Myb responsive promoter and a cell-specific Myb-inducible enhancer. Recently, it has been proven that two amino acid substitutions in a hydrophobic patch in the transactivation domain of v-Myb AMV are sufficient to disrupt its ability to stimulate the enhancer. This work focuses on the consequences of these amino acid substitutions by investigating protein-protein interactions of the hydrophobic region of v-Myb AMV in comparison to v Myb E26. Previous experiments identified GRP78 as an interaction partner of v Myb. In this study, a cytosolic variant of GRP78, GRP78va, was confirmed to interact with both v-Myb proteins. It was shown that its interaction site is limited to a very small region of v-Myb preceding the hydrophobic patch. Additionally, it was shown that GRP78va associated with all other members of the Myb-family and also with C/EBPß and HIPK2, suggesting a non-sequence-specific binding of GRP78va. Furthermore, reporter gene experiments demonstrated a repressing effect of GRP78va on the transactivation potential of v-Myb E26. In addition, GST pull down assays and co-immunoprecipitation experiments were used to precipitate endogenous proteins that could represent potential interaction partners of v-Myb. SDS-PAGE analysis revealed candidate bands, but mass spectrometry analysis failed to identify any proteins relevant for interaction with v Myb. Two other proteins were tested for their interaction with the hydrophobic patch of v-Myb. Co-immunoprecipitation experiments confirmed that C/EBPß interacts with the hydrophobic region of v-Myb and that the amino acid substitutions seem to affect the interaction in a negative way. Furthermore, PRMT4 was identified as an interaction partner of v-Myb. Mapping experiments showed the interaction to be mediated by the hydrophobic region. The point mutations in v-Myb AMV appear to positively influence the affinity for PRMT4. The fact that a SUMO binding motif is located in the same region might suggest a potential involvement of SUMO in the interaction of PRMT4 and v-Myb. Buch 22.0 x 15.5 x 0.8 cm , Diplomica Verlag, Diplomica Verlag<

2012, ISBN: 9783842882911

Taschenbuch

Diplomica Verlag, Taschenbuch, Auflage: 1., 120 Seiten, Publiziert: 2012-08-31T00:00:01Z, Produktgruppe: Buch, Hersteller-Nr.: black & white illustrations, 0.34 kg, Ingenieurwissenschafte… Mehr…

Diplomica Verlag, Taschenbuch, Auflage: 1., 120 Seiten, Publiziert: 2012-08-31T00:00:01Z, Produktgruppe: Buch, Hersteller-Nr.: black & white illustrations, 0.34 kg, Ingenieurwissenschaften, Fachbücher, Kategorien, Bücher, Biotechnologie, Medizin & Gesundheitsdienste, Ingenieurwissenschaft & Technik, Naturwissenschaften & Technik, Allgemein, Biologie, Biowissenschaften, Genetik, Fremdsprachige Bücher, Featured Categories, Englische Bücher, 7c9a6c79-19ea-4dea-90da-d7d47042d341_2301, 7c9a6c79-19ea-4dea-90da-d7d47042d341_0, Arborist Merchandising Root, acc906d0-2585-4921-a56f-3ff277850936_4901, acc906d0-2585-4921-a56f-3ff277850936_0, Special Features Stores, Taschenbücher, acc906d0-2585-4921-a56f-3ff277850936_4201, Diplomica Verlag, 2012<

2009, ISBN: 9783842882911

Softcover, PLEASE NOTE, WE DO NOT SHIP TO DENMARK. New Book. Shipped from UK in 4 to 14 days. Established seller since 2000. Please note we cannot offer an expedited shipping service from… Mehr…

Softcover, PLEASE NOTE, WE DO NOT SHIP TO DENMARK. New Book. Shipped from UK in 4 to 14 days. Established seller since 2000. Please note we cannot offer an expedited shipping service from the UK., [PU: Diplomica]<

ISBN: 9783842882911

Paperback. New., 6