Abstract
Nucleophosmin (B23) was phosphorylated in vitro with [gamma-32P]ATP and a nuclear kinase (type II) purified from HeLa cells. The phosphorylation was inhibited by heparin and by 2,3-diphosphoglycerate. Peptide mapping analysis indicated that the phosphorylation site in vitro was identical to that in vivo. Purified nucleoli have a similar kinase that phosphorylated nucleophosmin at the same site. These results indicated that nucleophosmin is phosphorylated in vivo by a nucleolar kinase (type II).
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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2,3-Diphosphoglycerate
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Amino Acid Sequence
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Binding Sites
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Cell Nucleolus / enzymology
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Cell Nucleus / enzymology*
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Diphosphoglyceric Acids / pharmacology
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HeLa Cells
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Heparin / pharmacology
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Humans
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Molecular Sequence Data
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Nuclear Proteins / metabolism*
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Nucleophosmin
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Peptide Mapping
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Phosphorylation
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Protein Kinases / metabolism*
Substances
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Diphosphoglyceric Acids
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NPM1 protein, human
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Nuclear Proteins
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Nucleophosmin
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2,3-Diphosphoglycerate
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Heparin
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Protein Kinases
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protein kinase NII