Specificity of ATP-dependent and GTP-dependent protein kinases with respect to ribosomal proteins of Escherichia coli

O G Issinger, M C Kiefer, R R Traut

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1975-Nov-1
OriginalsprogEngelsk
TidsskriftEuropean Journal of Biochemistry
Vol/bind59
Udgave nummer1
Sider (fra-til)137-143
Antal sider6
ISSN0014-2956
StatusUdgivet - 1. nov. 1975

Fingeraftryk

Ribosomal Proteins
Proteins
Rabbits
S 6
Muscle Proteins
Reticulocytes
Protein S
Protein Subunits
Catalytic Domain
Skeletal Muscle

Citer dette

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title = "Specificity of ATP-dependent and GTP-dependent protein kinases with respect to ribosomal proteins of Escherichia coli",
abstract = "Two protein kinases differing in substrate specificity were used to phosphorylate the 30-S and the 50-S ribosomal subunits of Escherichia coli. The catalytic subunit from the rabbit skeletal muscle protein kinase phosphorylates proteins S1, S4, S9, S13 and S18 of the 30-S subunit and proteins L2, L4, L5, L16, L18 and L23 of the 50-S subunit with (gamma-32P)ATP as phosphoryl donor. A second protein kinase isolated from rabbit reticulocytes, formerly shown to phosphorylate preferentially acidic proteins and to use GTP as well as ATP, strongly phosphorylated protein S6, an acidic protein of the small ribosomal subunit, and to a lesser extent proteins L7 and L12 or the large subunit. Evidence is presented showing different phosphorylation patterns when either whole subunits or the extracted proteins were used as substrate for the protein kinase. Kinetic studies showed proteins S1 and S4 to become most rapidly phosphorylated. Although most proteins incorporated less than stoichiometric amounts of phosphate, it is shown that with a high excess of ATP L2 bound 1 mol phosphate/mol protein.",
keywords = "Adenosine Triphosphate, Animals, Enzyme Activation, Escherichia coli, Guanosine Triphosphate, Muscles, Organ Specificity, Protein Kinases, Rabbits, Reticulocytes, Ribosomal Proteins",
author = "Issinger, {O G} and Kiefer, {M C} and Traut, {R R}",
year = "1975",
month = "11",
day = "1",
language = "English",
volume = "59",
pages = "137--143",
journal = "European Journal of Biochemistry",
issn = "0014-2956",
publisher = "AAAI Press",
number = "1",

}

Specificity of ATP-dependent and GTP-dependent protein kinases with respect to ribosomal proteins of Escherichia coli. / Issinger, O G; Kiefer, M C; Traut, R R.

I: European Journal of Biochemistry, Bind 59, Nr. 1, 01.11.1975, s. 137-143.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Specificity of ATP-dependent and GTP-dependent protein kinases with respect to ribosomal proteins of Escherichia coli

AU - Issinger, O G

AU - Kiefer, M C

AU - Traut, R R

PY - 1975/11/1

Y1 - 1975/11/1

N2 - Two protein kinases differing in substrate specificity were used to phosphorylate the 30-S and the 50-S ribosomal subunits of Escherichia coli. The catalytic subunit from the rabbit skeletal muscle protein kinase phosphorylates proteins S1, S4, S9, S13 and S18 of the 30-S subunit and proteins L2, L4, L5, L16, L18 and L23 of the 50-S subunit with (gamma-32P)ATP as phosphoryl donor. A second protein kinase isolated from rabbit reticulocytes, formerly shown to phosphorylate preferentially acidic proteins and to use GTP as well as ATP, strongly phosphorylated protein S6, an acidic protein of the small ribosomal subunit, and to a lesser extent proteins L7 and L12 or the large subunit. Evidence is presented showing different phosphorylation patterns when either whole subunits or the extracted proteins were used as substrate for the protein kinase. Kinetic studies showed proteins S1 and S4 to become most rapidly phosphorylated. Although most proteins incorporated less than stoichiometric amounts of phosphate, it is shown that with a high excess of ATP L2 bound 1 mol phosphate/mol protein.

AB - Two protein kinases differing in substrate specificity were used to phosphorylate the 30-S and the 50-S ribosomal subunits of Escherichia coli. The catalytic subunit from the rabbit skeletal muscle protein kinase phosphorylates proteins S1, S4, S9, S13 and S18 of the 30-S subunit and proteins L2, L4, L5, L16, L18 and L23 of the 50-S subunit with (gamma-32P)ATP as phosphoryl donor. A second protein kinase isolated from rabbit reticulocytes, formerly shown to phosphorylate preferentially acidic proteins and to use GTP as well as ATP, strongly phosphorylated protein S6, an acidic protein of the small ribosomal subunit, and to a lesser extent proteins L7 and L12 or the large subunit. Evidence is presented showing different phosphorylation patterns when either whole subunits or the extracted proteins were used as substrate for the protein kinase. Kinetic studies showed proteins S1 and S4 to become most rapidly phosphorylated. Although most proteins incorporated less than stoichiometric amounts of phosphate, it is shown that with a high excess of ATP L2 bound 1 mol phosphate/mol protein.

KW - Adenosine Triphosphate

KW - Animals

KW - Enzyme Activation

KW - Escherichia coli

KW - Guanosine Triphosphate

KW - Muscles

KW - Organ Specificity

KW - Protein Kinases

KW - Rabbits

KW - Reticulocytes

KW - Ribosomal Proteins

M3 - Journal article

VL - 59

SP - 137

EP - 143

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

SN - 0014-2956

IS - 1

ER -