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

F Meggio, B Boldyreff, O G Issinger, L A Pińna

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1994-Apr-12
OriginalsprogEngelsk
TidsskriftBiochemistry
Vol/bind33
Udgave nummer14
Sider (fra-til)4336-4342
Antal sider6
ISSN0006-2960
StatusUdgivet - 12. apr. 1994

Fingeraftryk

Casein Kinase II
Calmodulin
Down-Regulation
Chemical activation
Holoenzymes
Polylysine
Bearings (structural)
Peptides
Histones
Substrates
Phosphorylation
Salmine
Substitution reactions
Calcium-Calmodulin-Dependent Protein Kinases
Polyamines
Catalytic Domain
Mutation

Citer dette

@article{a5c8a9b05a4811de839d000ea68e967b,
title = "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",
abstract = "The noncatalytic beta-subunit is responsible for the latency of casein kinase 2 (CK2) activity toward calmodulin. Twenty-one mutants of the beta-subunit bearing either deletions or Ala substitutions for charged residues in the 5-6, 55-70, and 171-178 sequences have been assayed for their ability to substitute for wild-type beta-subunit as a suppressor of activity toward calmodulin. The only mutations that reduced the ability of the beta-subunit to suppress calmodulin phosphorylation activity, though being compatible with normal reconstitution of CK2 holoenzyme, were those affecting Asp55, Glu57 and the whole triplet Glu59-Asp-Glu61. The activity of CK2 holoenzyme, either native or reconstituted, toward calmodulin can be elicited by a variety of polybasic effectors, including polylysine, polyarginine, salmine, and histones H4, H3, and, to a lesser extent, H2a and H2b. Histone H1 and polyamines are conversely ineffective. The latent {"}calmodulin kinase{"} activity of CK2 can also be specifically unmasked by a peptide (alpha[66-86]) reproducing a basic insert of the catalytic subunit. This effect is reversed by equimolar addition of a peptide (beta[55-71]) including the 55-64 acidic stretch of the beta-subunit. Comparable polylysine stimulation was observed with the holoenzymes reconstituted with either beta wt or the beta mutants capable of assembling with the alpha-subunit, with the notable exception of those bearing Ala substitutions for acidic residues at positions 55, 57, and 59-61. These were nearly insensitive to 42 nM polylysine, which conversely promotes a more than 10-fold increase of calmodulin phosphorylation with wild-type beta.(ABSTRACT TRUNCATED AT 250 WORDS)",
keywords = "Amino Acid Sequence, Calmodulin, Casein Kinases, Down-Regulation, Enzyme Activation, Hydrogen-Ion Concentration, Molecular Sequence Data, Mutation, Peptide Fragments, Phosphorylation, Polyamines, Polymers, Protein Kinases",
author = "F Meggio and B Boldyreff and Issinger, {O G} and Pińna, {L A}",
year = "1994",
month = "4",
day = "12",
language = "English",
volume = "33",
pages = "4336--4342",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "14",

}

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. / Meggio, F; Boldyreff, B; Issinger, O G; Pińna, L A.

I: Biochemistry, Bind 33, Nr. 14, 12.04.1994, s. 4336-4342.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - 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

AU - Meggio, F

AU - Boldyreff, B

AU - Issinger, O G

AU - Pińna, L A

PY - 1994/4/12

Y1 - 1994/4/12

N2 - The noncatalytic beta-subunit is responsible for the latency of casein kinase 2 (CK2) activity toward calmodulin. Twenty-one mutants of the beta-subunit bearing either deletions or Ala substitutions for charged residues in the 5-6, 55-70, and 171-178 sequences have been assayed for their ability to substitute for wild-type beta-subunit as a suppressor of activity toward calmodulin. The only mutations that reduced the ability of the beta-subunit to suppress calmodulin phosphorylation activity, though being compatible with normal reconstitution of CK2 holoenzyme, were those affecting Asp55, Glu57 and the whole triplet Glu59-Asp-Glu61. The activity of CK2 holoenzyme, either native or reconstituted, toward calmodulin can be elicited by a variety of polybasic effectors, including polylysine, polyarginine, salmine, and histones H4, H3, and, to a lesser extent, H2a and H2b. Histone H1 and polyamines are conversely ineffective. The latent "calmodulin kinase" activity of CK2 can also be specifically unmasked by a peptide (alpha[66-86]) reproducing a basic insert of the catalytic subunit. This effect is reversed by equimolar addition of a peptide (beta[55-71]) including the 55-64 acidic stretch of the beta-subunit. Comparable polylysine stimulation was observed with the holoenzymes reconstituted with either beta wt or the beta mutants capable of assembling with the alpha-subunit, with the notable exception of those bearing Ala substitutions for acidic residues at positions 55, 57, and 59-61. These were nearly insensitive to 42 nM polylysine, which conversely promotes a more than 10-fold increase of calmodulin phosphorylation with wild-type beta.(ABSTRACT TRUNCATED AT 250 WORDS)

AB - The noncatalytic beta-subunit is responsible for the latency of casein kinase 2 (CK2) activity toward calmodulin. Twenty-one mutants of the beta-subunit bearing either deletions or Ala substitutions for charged residues in the 5-6, 55-70, and 171-178 sequences have been assayed for their ability to substitute for wild-type beta-subunit as a suppressor of activity toward calmodulin. The only mutations that reduced the ability of the beta-subunit to suppress calmodulin phosphorylation activity, though being compatible with normal reconstitution of CK2 holoenzyme, were those affecting Asp55, Glu57 and the whole triplet Glu59-Asp-Glu61. The activity of CK2 holoenzyme, either native or reconstituted, toward calmodulin can be elicited by a variety of polybasic effectors, including polylysine, polyarginine, salmine, and histones H4, H3, and, to a lesser extent, H2a and H2b. Histone H1 and polyamines are conversely ineffective. The latent "calmodulin kinase" activity of CK2 can also be specifically unmasked by a peptide (alpha[66-86]) reproducing a basic insert of the catalytic subunit. This effect is reversed by equimolar addition of a peptide (beta[55-71]) including the 55-64 acidic stretch of the beta-subunit. Comparable polylysine stimulation was observed with the holoenzymes reconstituted with either beta wt or the beta mutants capable of assembling with the alpha-subunit, with the notable exception of those bearing Ala substitutions for acidic residues at positions 55, 57, and 59-61. These were nearly insensitive to 42 nM polylysine, which conversely promotes a more than 10-fold increase of calmodulin phosphorylation with wild-type beta.(ABSTRACT TRUNCATED AT 250 WORDS)

KW - Amino Acid Sequence

KW - Calmodulin

KW - Casein Kinases

KW - Down-Regulation

KW - Enzyme Activation

KW - Hydrogen-Ion Concentration

KW - Molecular Sequence Data

KW - Mutation

KW - Peptide Fragments

KW - Phosphorylation

KW - Polyamines

KW - Polymers

KW - Protein Kinases

M3 - Journal article

VL - 33

SP - 4336

EP - 4342

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 14

ER -