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Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II.

作者信息

Palvimo J, Linnala-Kankkunen A

机构信息

Department of Biochemistry, University of Kuopio, Finland.

出版信息

FEBS Lett. 1989 Oct 23;257(1):101-4. doi: 10.1016/0014-5793(89)81796-x.

DOI:10.1016/0014-5793(89)81796-x
PMID:2806554
Abstract

The amino acid sequence of a region on chromosomal protein HMG-I from human cells that is phosphorylated by casein kinase II has been determined. The sequence is: Leu-Glu-Lys-Glu-Glu-Glu-Glu-Gly-Ile-Ser-Gln-Glu-Ser(P)-Ser(P)-Glu-Glu-Gl u-Gln. It corresponds to the C-terminal residues 90-107 of HMG-I [(1989) Mol. Cell. Biol. 9, 2114-2123]. Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells.

摘要

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