Identification of significant regions of transcription factor DP-1 (TFDP-1) involved in stability/instability of the protein |
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Authors: | Takashi Arakawa Yoshiaki Kamiya |
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Affiliation: | Department of Applied Biological Sciences, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-city, Kanagawa 252-8510, Japan |
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Abstract: | We previously reported the identification of DP-1 isoforms (α and β), which are structurally C-terminus-deleted ones, and revealed the low-level expression of these isoforms. It is known that wild-type DP-1 is degraded by the ubiquitin-proteasome system, but few details are known about the domains concerned with the protein stability/instability for the proteolysis of these DP-1 isoforms. Here we identified the domains responsible for the stability/instability of DP-1. Especially, the DP-1 “Stabilon” domain was a C-terminal acidic motif and was quite important for DP-1 stability. Moreover, we propose that this DP-1 Stabilon may be useful for the stability of other nuclear proteins when fused to them. |
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Keywords: | DP-1, E2F dimerization partner 1 RT-PCR, reverse transcription-polymerase chain reaction HEK, human embryonic kidney piPSCs, protein-induced pluripotent stem cells HA, hemagglutinin DBD, DNA-binding domain ER, estrogen receptor WT, wild type |
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