Unique features of HIV‐1 Rev protein phosphorylation by protein kinase CK2 (‘casein kinase‐2’)

FEBS Letters

Pagano, Mario A²  Ciminale, Vincenzo¹  Pinna, Lorenzo A²  Boschetti, Marco²  D'Agostino, Donna M¹  Sarno, Stefania²  Marin, Oriano²  Meggio, Flavio² 

[1] Dipartimento di Scienze Oncologiche e Chirurgiche, Sezione di Oncologia, Università degli Studi di Padova, via Gattamelata 64, 35128 Padua, Italy;Dipartimento di Chimica Biologica and Centro del CNR per lo Studio delle Biomembrane, Università degli Studi di Padova, viale G. Colombo 3, 35121 Padua, Italy

关键词: Casein kinase-2;    Protein kinase;    Protein phosphorylation;    Human immunodeficiency virus type-1;    Rev;    CK2;    casein kinase-2;    HIV-1;    human immunodeficiency virus type-1;   

DOI  :  10.1016/S0014-5793(00)01971-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The HIV-1 Rev transactivator is phosphorylated in vitro by protein kinase CK2 at two residues, Ser-5 and Ser-8; these sites are also phosphorylated in vivo. Here we show that the mechanism by which CK2 phosphorylates Rev is unique in several respects, notably: (i) it is fully dependent on the regulatory, β-subunit of CK2; (ii) it relies on the integrity of an acidic stretch of CK2β which down-regulates the phosphorylation of other substrates; (iii) it is inhibited in a dose-dependent manner by polyamines and other polycationic effectors that normally stimulate CK2 activity. In contrast, a peptide corresponding to the amino-terminal 26 amino acids of Rev, including the phosphoacceptor site, is readily phosphorylated by the catalytic subunit of CK2 even in the absence of the β-subunit. These data, in conjunction with the observation that two functionally inactive derivatives of Rev with mutations in its helix-loop-helix motif are refractory to phosphorylation, indicate the phosphorylation of Rev by CK2 relies on conformational features of distinct regions that are also required for the transactivator's biological activity.

【 授权许可】

Unknown