Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown.

A. Hershko, Aaron Ciechanover, I. A. Rose

Research output: Contribution to journalArticle

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Abstract

The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide, the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde, and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography. These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.

Original languageEnglish
Pages (from-to)1525-1528
Number of pages4
JournalJournal of Biological Chemistry
Volume256
Issue number4
StatePublished - 25 Feb 1981

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Adenosine Triphosphate
Amino Acids
Peptides
Thin layer chromatography
Borohydrides
Proteins
Ethanolamine
Thin Layer Chromatography
Chromatography
Electrophoresis
Glycine
Formaldehyde
Hydrolysis
Hot Temperature
Derivatives
Acids
metaperiodate

Cite this

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abstract = "The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide, the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde, and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography. These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.",
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Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown. / Hershko, A.; Ciechanover, Aaron; Rose, I. A.

In: Journal of Biological Chemistry, Vol. 256, No. 4, 25.02.1981, p. 1525-1528.

Research output: Contribution to journalArticle

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AU - Ciechanover, Aaron

AU - Rose, I. A.

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N2 - The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide, the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde, and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography. These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.

AB - The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide, the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde, and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography. These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.

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