FEBS Letters | |
Prothymosin α is phosphorylated by casein kinase‐2 | |
Barcia, Miguel G.1  Jullien, Cristina D.1  Freire, Manuel1  Castro, José M.1  González, Carlos G.1  | |
[1] Departamento de Bioquímica e Bioloxía Molecular, Facultade de Bioloxía, Universidade de Santiago de Compostela, Galicia, Spain | |
关键词: Prothymosin α; Thymosin α1; Casein kinase-2; EGTA; [ethylenebis(oxyethylenenitrilo)]tetraacetic acid; CK-2; casein kinase-2; ProTα; prothymosin α; Tα1; thymosin α1; HPLC; high performance liquid chromatography; | |
DOI : 10.1016/0014-5793(92)80924-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Prothymosin α (ProTα) is a 12.5 kDa acidic polypeptide that is considered to have a nuclear function related to cell proliferation. Inspection of its amino acid sequence revealed the presence of sequences that may serve as targets for phosphorylation by casein kinase-2 (CK-2). ProTα isolated from calf thymocytes was phosphorylated in vitro by CK-2. The phosphorylation sites are Ser and Thr residues located among the first 14 amino acid residues in the ProTα sequence. Another site that is theoretically suitable for phosphorylation by CK-2, at the C-terminus of the polypeptide, is not, in fact, phosphorylated. Thymosin α1 (Tα1), a peptide whose sequence corresponds to the first 28 amino acids of ProTα, is also phosphorylated by CK-2 at the same phosphorylation sites as ProTα. In cultured splenic lymphocytes ProTα was phosphorylated at Thr residues located at positions 7, 12 and/or 13. Based on these observations we conclude that CK-2, or another cellular kinase with similar sequence specifity, is responsible for phosphorylation of ProTα in vivo.
【 授权许可】
Unknown
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