An ARID family protein binds to the African swine fever virus encoded ubiquitin conjugating enzyme, UBCv1

FEBS Letters

Dixon, Linda K.¹  Bulimo, Wallace D.¹  Miskin, James E.¹ 

[1] Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Surrey GU24 0NF, UK

关键词: Ubiquitin conjugating enzyme;    African swine fever virus;    A/T rich interaction domain;    Ubiquitin;    SMCX;   

DOI  :  10.1016/S0014-5793(00)01352-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The NH₂-terminal end of a protein, named SMCp, which contains an ARID (A/T rich interaction domain) DNA binding domain and is similar to the mammalian SMCY/SMCX proteins and retinoblastoma binding protein 2, was shown to bind the African swine fever virus encoded ubiquitin conjugating enzyme (UBCv1) using the yeast two hybrid system and in in vitro binding assays. Antisera raised against the SMCp protein were used to show that the protein is present in the cell nucleus. Immunofluorescence showed that although UBCv1 is present in the nucleus in most cells, in some cells it is in the cytoplasm, suggesting that it shuttles between the nucleus and cytoplasm. The interaction and co-localisation of UBCv1 with SMCp suggest that SMCp may be a substrate in vivo for the enzyme.

【 授权许可】

Unknown