Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides.
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Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides. / Hilz, H; Koch, R; Fanick, Werner; Klapproth, K; Adamietz, P.
In: P NATL ACAD SCI USA, Vol. 81, No. 13, 13, 1984, p. 3929-3933.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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T1 - Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides.
AU - Hilz, H
AU - Koch, R
AU - Fanick, Werner
AU - Klapproth, K
AU - Adamietz, P
PY - 1984
Y1 - 1984
N2 - The apparent NAD:protein ADP-ribosyl transferase activity of mitochondria and submitochondrial particles from beef heart and rat liver is simulated by a reaction sequence that consists of an enzymic hydrolysis of NAD to ADP-ribose (ADP-Rib) by NAD glycohydrolase(s) and a nonenzymic ADP-ribosylation of acceptor proteins by the free ADP-Rib formed. The nonenzymic ADP-ribosylation of mitochondrial proteins showed two pH optima and exhibited the same remarkable selectivity as the reaction with NAD. The predominant acceptor in beef heart mitochondria was a 30-kDa protein, whereas in mitochondrial extracts of rat liver a 50-55 kDa polypeptide served as an acceptor. No authentic ADP-Rib transferase activity could be detected even when free ADP-Rib was trapped by NH2OH. Once formed, the mitochondrial ADP-Rib conjugates were resistant to hydroxylamine. NH2OH-resistant mono(ADP-Rib)-protein conjugates as found in most cells may also be products of nonenzymic ADP-ribosylation. In mouse tissues, their amounts relate to protein and NAD contents, and they increase specifically and reversibly in the hypothyroid status. Furthermore, intact rat liver mitochondria contain a mono(ADP-Rib)-polypeptide (50-55 kDa) that appeared to be identical with the polypeptide reacting with ADP-Rib in vitro.
AB - The apparent NAD:protein ADP-ribosyl transferase activity of mitochondria and submitochondrial particles from beef heart and rat liver is simulated by a reaction sequence that consists of an enzymic hydrolysis of NAD to ADP-ribose (ADP-Rib) by NAD glycohydrolase(s) and a nonenzymic ADP-ribosylation of acceptor proteins by the free ADP-Rib formed. The nonenzymic ADP-ribosylation of mitochondrial proteins showed two pH optima and exhibited the same remarkable selectivity as the reaction with NAD. The predominant acceptor in beef heart mitochondria was a 30-kDa protein, whereas in mitochondrial extracts of rat liver a 50-55 kDa polypeptide served as an acceptor. No authentic ADP-Rib transferase activity could be detected even when free ADP-Rib was trapped by NH2OH. Once formed, the mitochondrial ADP-Rib conjugates were resistant to hydroxylamine. NH2OH-resistant mono(ADP-Rib)-protein conjugates as found in most cells may also be products of nonenzymic ADP-ribosylation. In mouse tissues, their amounts relate to protein and NAD contents, and they increase specifically and reversibly in the hypothyroid status. Furthermore, intact rat liver mitochondria contain a mono(ADP-Rib)-polypeptide (50-55 kDa) that appeared to be identical with the polypeptide reacting with ADP-Rib in vitro.
KW - Animals
KW - Kinetics
KW - Cattle
KW - Electrophoresis, Polyacrylamide Gel
KW - Molecular Weight
KW - Adenosine Diphosphate Ribose/metabolism
KW - NAD/metabolism
KW - Mitochondria/metabolism
KW - Mitochondria, Heart/metabolism
KW - Nucleoside Diphosphate Sugars/metabolism
KW - Peptides/isolation & purification/metabolism
KW - Submitochondrial Particles/metabolism
KW - Tritium/diagnostic use
KW - Animals
KW - Kinetics
KW - Cattle
KW - Electrophoresis, Polyacrylamide Gel
KW - Molecular Weight
KW - Adenosine Diphosphate Ribose/metabolism
KW - NAD/metabolism
KW - Mitochondria/metabolism
KW - Mitochondria, Heart/metabolism
KW - Nucleoside Diphosphate Sugars/metabolism
KW - Peptides/isolation & purification/metabolism
KW - Submitochondrial Particles/metabolism
KW - Tritium/diagnostic use
M3 - SCORING: Journal article
VL - 81
SP - 3929
EP - 3933
JO - P NATL ACAD SCI USA
JF - P NATL ACAD SCI USA
SN - 0027-8424
IS - 13
M1 - 13
ER -