Literature DB >> 10094389

Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance.

M J Benitez1, G Mier, F Brione, F J Moreno, J S Jiménez.   

Abstract

The interaction between protein kinase CK2 and polylysine has been studied by Surface Plasmon Resonance (SPR). The binding process has a very low energy of activation, it is irreversible, and too slow as to explain the enzyme activity stimulation as a direct consequence of the polylysine binding. The polylysine interaction with a peptide substrate and with casein are faster, and in agreement with a substrate-mediated mechanism of activity stimulation. After several hours of incubation, the binding of polylysine to CK2 produces the loss of enzymatic activity.

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Year:  1999        PMID: 10094389

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  25 in total

Review 1.  Casein kinase 2: an 'eminence grise' in cellular regulation?

Authors:  L A Pinna
Journal:  Biochim Biophys Acta       Date:  1990-09-24

2.  The effect of polylysine on casein-kinase-2 activity is influenced by both the structure of the protein/peptide substrates and the subunit composition of the enzyme.

Authors:  F Meggio; B Boldyreff; O Marin; F Marchiori; J W Perich; O G Issinger; L A Pinna
Journal:  Eur J Biochem       Date:  1992-05-01

Review 3.  Casein kinase I and II--multipotential serine protein kinases: structure, function, and regulation.

Authors:  P T Tuazon; J A Traugh
Journal:  Adv Second Messenger Phosphoprotein Res       Date:  1991

4.  A hepatic soluble cyclic nucleotide-independent protein kinase. Stimulation by basic polypeptides.

Authors:  M Yamamoto; W E Criss; Y Takai; H Yamamura; Y Nishizuka
Journal:  J Biol Chem       Date:  1979-06-25       Impact factor: 5.157

5.  A surface-plasmon-resonance analysis of polylysine interactions with a peptide substrate of protein kinase CK2 and with the enzyme.

Authors:  M J Benítez; G Mier; F Briones; F J Moreno; J S Jiménez
Journal:  Biochem J       Date:  1997-06-15       Impact factor: 3.857

Review 6.  Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation.

Authors:  J E Allende; C C Allende
Journal:  FASEB J       Date:  1995-03       Impact factor: 5.191

7.  Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate.

Authors:  F Meggio; B Boldyreff; O G Issinger; L A Pińna
Journal:  Biochemistry       Date:  1994-04-12       Impact factor: 3.162

Review 8.  Casein kinases--multipotential protein kinases.

Authors:  G M Hathaway; J A Traugh
Journal:  Curr Top Cell Regul       Date:  1982

9.  Autophosphorylation of type 2 casein kinase TS at both its alpha- and beta-subunits. Influence of different effectors.

Authors:  F Meggio; A M Brunati; L A Pinna
Journal:  FEBS Lett       Date:  1983-08-22       Impact factor: 4.124

10.  Structure of protein kinase CK2: dimerization of the human beta-subunit.

Authors:  B Boldyreff; U Mietens; O G Issinger
Journal:  FEBS Lett       Date:  1996-01-29       Impact factor: 4.124

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  1 in total

1.  A surface plasmon resonance study of the interactions between the component subunits of protein kinase CK2 and two protein substrates, casein and calmodulin.

Authors:  M J Benítez; C Cochet; J S Jiménez
Journal:  Mol Cell Biochem       Date:  2001-11       Impact factor: 3.396

  1 in total

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