Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C.

Abstract:

:CtBP has been shown to be a highly conserved corepressor of transcription. E1A and all the various transcription factors to which CtBP binds contain a conserved PLDLS CtBP-interacting domain, and EBNA3C includes a PLDLS motif (amino acids [aa] 728 to 732). Here we show that EBNA3C binds to CtBP both in vitro and in vivo and that the interaction requires an intact PLDLS. The C terminus of EBNA3C (aa 580 to 992) has modest trans-repressor activity when it is fused to the DNA-binding domain of Gal4, and deletion or mutation of the PLDLS sequence ablates this and unmasks a transactivation function within the fragment. However, loss of the CtBP interaction motif had little effect on the ability of full-length EBNA3C to repress transcription. A striking correlation between CtBP binding and the capacity of EBNA3C to cooperate with (Ha-)Ras in the immortalization and transformation of primary rat embryo fibroblasts was also revealed.

journal_name

J Virol

journal_title

Journal of virology

authors

Touitou R,Hickabottom M,Parker G,Crook T,Allday MJ

doi

10.1128/JVI.75.16.7749-7755.2001

subject

Has Abstract

pub_date

2001-08-01 00:00:00

pages

7749-55

issue

16

eissn

0022-538X

issn

1098-5514

journal_volume

75

pub_type

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