The identification in HeLa nuclei of a novel DNA-binding protein, designated HrpF, is presented. This factor recognizes and binds a sequence of the Xenopus Iaevis L14 ribosomal protein (r-p) gene promoter bound by the Xenopus r-p transcription factor I (XrpFl) (1). We show here that XrpFl and HrpF share a conserved DNA-binding domain. We also present evidences suggesting that the two factors perform similar functions in the cell. We discuss the hypothesis that closely related factors might be involved in the control of rp-gene transcription in vertebrates.
Lagna, G., Loreni, F., Beccari, E., & Carnevali, F. (1990). HrpF, a human sequence-specific DNA-binding protein homologous to XrpFl, a Xenopus Iaevis oocyte transcription factor. NUCLEIC ACIDS RESEARCH, 18(19), 5811-5816 [10.1093/nar/18.19.5811].
HrpF, a human sequence-specific DNA-binding protein homologous to XrpFl, a Xenopus Iaevis oocyte transcription factor
LORENI, FABRIZIO;
1990
Abstract
The identification in HeLa nuclei of a novel DNA-binding protein, designated HrpF, is presented. This factor recognizes and binds a sequence of the Xenopus Iaevis L14 ribosomal protein (r-p) gene promoter bound by the Xenopus r-p transcription factor I (XrpFl) (1). We show here that XrpFl and HrpF share a conserved DNA-binding domain. We also present evidences suggesting that the two factors perform similar functions in the cell. We discuss the hypothesis that closely related factors might be involved in the control of rp-gene transcription in vertebrates.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
