Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein.
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Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein. / Muñoz, A; Zenke, M; Gehring, U; Sap, J; Beug, H; Vennström, B.
I: EMBO Journal, Bind 7, Nr. 1, 1988, s. 155-9.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein.
AU - Muñoz, A
AU - Zenke, M
AU - Gehring, U
AU - Sap, J
AU - Beug, H
AU - Vennström, B
N1 - Keywords: Animals; Chickens; Chimera; Cloning, Molecular; Genes; Kinetics; Mutation; Plasmids; Protein Biosynthesis; Proto-Oncogenes; Receptors, Thyroid Hormone; Recombinant Proteins; Thyroid Hormones; Transcription, Genetic
PY - 1988
Y1 - 1988
N2 - To identify and characterize the hormone-binding domain of the thyroid hormone receptor, we analyzed the ligand-binding capacities of proteins representing chimeras between the normal receptor and P75gag-v-erbA, the retrovirus-encoded form deficient in binding ligand. Our results show that several mutations present in the carboxy-terminal half of P75gag-v-erbA co-operate in abolishing hormone binding, and that the ligand-binding domain resides in a position analogous to that of steroid receptors. Furthermore, a point mutation that is located between the putative DNA and ligand-binding domains of P75gag-v-erbA and that renders it biologically inactive fails to affect hormone binding by the c-erbA protein. These results suggest that the mutation changed the ability of P75gag-v-erbA to affect transcription since it also had no effect on DNA binding. Our data also suggest that hormone-independent activity of P75gag-v-erbA provided a selective advantage to the avian erythroblastosis virus during the original selection for a highly oncogenic strain of the virus.
AB - To identify and characterize the hormone-binding domain of the thyroid hormone receptor, we analyzed the ligand-binding capacities of proteins representing chimeras between the normal receptor and P75gag-v-erbA, the retrovirus-encoded form deficient in binding ligand. Our results show that several mutations present in the carboxy-terminal half of P75gag-v-erbA co-operate in abolishing hormone binding, and that the ligand-binding domain resides in a position analogous to that of steroid receptors. Furthermore, a point mutation that is located between the putative DNA and ligand-binding domains of P75gag-v-erbA and that renders it biologically inactive fails to affect hormone binding by the c-erbA protein. These results suggest that the mutation changed the ability of P75gag-v-erbA to affect transcription since it also had no effect on DNA binding. Our data also suggest that hormone-independent activity of P75gag-v-erbA provided a selective advantage to the avian erythroblastosis virus during the original selection for a highly oncogenic strain of the virus.
M3 - Journal article
C2 - 3359993
VL - 7
SP - 155
EP - 159
JO - E M B O Journal
JF - E M B O Journal
SN - 0261-4189
IS - 1
ER -
ID: 5070261