Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides.

Standard

Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides. / Hilz, H; Koch, R; Fanick, Werner; Klapproth, K; Adamietz, P.

in: P NATL ACAD SCI USA, Jahrgang 81, Nr. 13, 13, 1984, S. 3929-3933.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Hilz, H, Koch, R, Fanick, W, Klapproth, K & Adamietz, P 1984, 'Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides.', P NATL ACAD SCI USA, Jg. 81, Nr. 13, 13, S. 3929-3933. <http://www.ncbi.nlm.nih.gov/pubmed/6588374?dopt=Citation>

APA

Hilz, H., Koch, R., Fanick, W., Klapproth, K., & Adamietz, P. (1984). Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides. P NATL ACAD SCI USA, 81(13), 3929-3933. [13]. http://www.ncbi.nlm.nih.gov/pubmed/6588374?dopt=Citation

Vancouver

Hilz H, Koch R, Fanick W, Klapproth K, Adamietz P. Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides. P NATL ACAD SCI USA. 1984;81(13):3929-3933. 13.

Bibtex

@article{ce1fe73428b94756816cc9165545fd0b,
title = "Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides.",
abstract = "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.",
keywords = "Animals, Kinetics, Cattle, Electrophoresis, Polyacrylamide Gel, Molecular Weight, Adenosine Diphosphate Ribose/*metabolism, NAD/metabolism, Mitochondria/*metabolism, Mitochondria, Heart/*metabolism, Nucleoside Diphosphate Sugars/*metabolism, Peptides/isolation & purification/*metabolism, Submitochondrial Particles/*metabolism, Tritium/diagnostic use, Animals, Kinetics, Cattle, Electrophoresis, Polyacrylamide Gel, Molecular Weight, Adenosine Diphosphate Ribose/*metabolism, NAD/metabolism, Mitochondria/*metabolism, Mitochondria, Heart/*metabolism, Nucleoside Diphosphate Sugars/*metabolism, Peptides/isolation & purification/*metabolism, Submitochondrial Particles/*metabolism, Tritium/diagnostic use",
author = "H Hilz and R Koch and Werner Fanick and K Klapproth and P Adamietz",
year = "1984",
language = "English",
volume = "81",
pages = "3929--3933",
journal = "P NATL ACAD SCI USA",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "13",

}

RIS

TY - JOUR

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 -