p300/CBP acts as a coactivator of the cone-rod homeobox transcription factor.
CRX (cone-rod homeobox) is shown to play an important role on the photoreceptor cell maturation and maintenance. However, little is known about the molecular mechanism how CRX potentiates transcription. Here, we investigated the effect of several coactivators (p300/CBP, SRC-1, TIF2, and AIB1) on the transactivation function of CRX. The transient expression assay with a luciferase reporter gene showed that only p300/CBP potentiates the transactivation function of CRX. Furthermore, by interaction studies in vivo (a mammalian two-hybrid assay) and in vitro (a pulldown assay), p300/CBP was found to directly bind CRX through their C-terminal domains. The C-terminal domain of CRX was mapped as a transactivation domain to associate with p300/CBP. Taken together, our results demonstrate that p300/CBP acts as one of the coactivators of CRX.
Yanagi
Y
Y
Department of Ophthalmology, University of Tokyo School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8655, Japan.
Masuhiro
Y
Y
Mori
M
M
Yanagisawa
J
J
Kato
S
S
D000818:Animals; D050881:E1A-Associated p300 Protein; D018398:Homeodomain Proteins / Q000378:metabolism*; D051379:Mice; D009687:Nuclear Proteins / Q000502:physiology*; D015534:Trans-Activators / Q000378:metabolism* / Q000502:physiology*
D018398:Homeodomain Proteins; D009687:Nuclear Proteins; D015534:Trans-Activators; C109288:cone rod homeobox protein; D050881:E1A-Associated p300 Protein; C494361:Ep300 protein, mouse