Identification of significant regions of transcription factor DP-1 (TFDP-1) involved in stability/instability of the protein.
We previously reported the identification of DP-1 isoforms (alpha and beta), 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.
Department of Applied Biological Sciences, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-city, Kanagawa 252-8510, Japan.
Takashi
T
Arakawa
Yoshikazu
Y
Masuhiro
Yoshiaki
Y
Kamiya
Hirohisa
H
Kojima
Shigemasa
S
Hanazawa
D020816:Amino Acid Motifs; D006801:Humans; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D050680:Transcription Factor DP1 / Q000235:genetics / Q000378:metabolism*
D009687:Nuclear Proteins; D020033:Protein Isoforms; D011993:Recombinant Fusion Proteins; C493735:TFDP1 protein, human; D050680:Transcription Factor DP1