Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase

Rafal Zieliński; Marek Pilecki; Konrad Kubiński; Piotr Zień; Ulf Hellman; Ryszard Szyszka

doi:10.1016/S0006-291X(02)02081-8

Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase

Rafal Zieliński, Marek Pilecki, Konrad Kubiński, Piotr Zień, Ulf Hellman, Ryszard Szyszka

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Reversible phosphorylation of acidic ribosomal proteins of Saccharomyces cerevisiae is an important mechanism, regulating the number of active ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. A new protein-inhibitor regulating activity of PK60S kinase has been purified from yeast extracts and characterised. Peptide mass fingerprinting (PMF) and amino-acid sequence analysis by Post Source Decay (PSD) have identified the inhibitor as a Cu-Zn superoxide dismutase (SOD). Inhibition by SOD is competitive with respect to protein substrates - P proteins and 80S ribosome - with K_i values of 3.7 μM for P2A protein and 0.6 μM for 80S ribosomes. A close correlation was found between the state of phosphorylation of P proteins in diauxic shift and logarithmic growth yeast cells and activity of SOD. The possible mechanism of regulation of PK60S activity, and participation of SOD protein in regulation of 80S-ribosome activity in stress conditions, is discussed.

Original language	English (US)
Pages (from-to)	1310-1316
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	296
Issue number	5
DOIs	https://doi.org/10.1016/S0006-291X(02)02081-8
State	Published - 2002
Externally published	Yes

Keywords

Cu-Zn superoxide dismutase
Inhibitory activity
P1/P2 proteins
Protein kinases
Ribosome phosphorylation
Yeast

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(02)02081-8

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title = "Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase",

abstract = "Reversible phosphorylation of acidic ribosomal proteins of Saccharomyces cerevisiae is an important mechanism, regulating the number of active ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. A new protein-inhibitor regulating activity of PK60S kinase has been purified from yeast extracts and characterised. Peptide mass fingerprinting (PMF) and amino-acid sequence analysis by Post Source Decay (PSD) have identified the inhibitor as a Cu-Zn superoxide dismutase (SOD). Inhibition by SOD is competitive with respect to protein substrates - P proteins and 80S ribosome - with Ki values of 3.7 μM for P2A protein and 0.6 μM for 80S ribosomes. A close correlation was found between the state of phosphorylation of P proteins in diauxic shift and logarithmic growth yeast cells and activity of SOD. The possible mechanism of regulation of PK60S activity, and participation of SOD protein in regulation of 80S-ribosome activity in stress conditions, is discussed.",

keywords = "Cu-Zn superoxide dismutase, Inhibitory activity, P1/P2 proteins, Protein kinases, Ribosome phosphorylation, Yeast",

author = "Rafal Zieli{\'n}ski and Marek Pilecki and Konrad Kubi{\'n}ski and Piotr Zie{\'n} and Ulf Hellman and Ryszard Szyszka",

year = "2002",

doi = "10.1016/S0006-291X(02)02081-8",

language = "English (US)",

volume = "296",

pages = "1310--1316",

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T1 - Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase

AU - Zieliński, Rafal

AU - Pilecki, Marek

AU - Kubiński, Konrad

AU - Zień, Piotr

AU - Hellman, Ulf

AU - Szyszka, Ryszard

PY - 2002

Y1 - 2002

N2 - Reversible phosphorylation of acidic ribosomal proteins of Saccharomyces cerevisiae is an important mechanism, regulating the number of active ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. A new protein-inhibitor regulating activity of PK60S kinase has been purified from yeast extracts and characterised. Peptide mass fingerprinting (PMF) and amino-acid sequence analysis by Post Source Decay (PSD) have identified the inhibitor as a Cu-Zn superoxide dismutase (SOD). Inhibition by SOD is competitive with respect to protein substrates - P proteins and 80S ribosome - with Ki values of 3.7 μM for P2A protein and 0.6 μM for 80S ribosomes. A close correlation was found between the state of phosphorylation of P proteins in diauxic shift and logarithmic growth yeast cells and activity of SOD. The possible mechanism of regulation of PK60S activity, and participation of SOD protein in regulation of 80S-ribosome activity in stress conditions, is discussed.

AB - Reversible phosphorylation of acidic ribosomal proteins of Saccharomyces cerevisiae is an important mechanism, regulating the number of active ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. A new protein-inhibitor regulating activity of PK60S kinase has been purified from yeast extracts and characterised. Peptide mass fingerprinting (PMF) and amino-acid sequence analysis by Post Source Decay (PSD) have identified the inhibitor as a Cu-Zn superoxide dismutase (SOD). Inhibition by SOD is competitive with respect to protein substrates - P proteins and 80S ribosome - with Ki values of 3.7 μM for P2A protein and 0.6 μM for 80S ribosomes. A close correlation was found between the state of phosphorylation of P proteins in diauxic shift and logarithmic growth yeast cells and activity of SOD. The possible mechanism of regulation of PK60S activity, and participation of SOD protein in regulation of 80S-ribosome activity in stress conditions, is discussed.

KW - Cu-Zn superoxide dismutase

KW - Inhibitory activity

KW - P1/P2 proteins

KW - Protein kinases

KW - Ribosome phosphorylation

KW - Yeast

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U2 - 10.1016/S0006-291X(02)02081-8

DO - 10.1016/S0006-291X(02)02081-8

M3 - Article

C2 - 12207917

AN - SCOPUS:0036387089

SN - 0006-291X

VL - 296

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EP - 1316

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 5

ER -

Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase

Abstract

Keywords

ASJC Scopus subject areas

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