The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity

Margarita Sandigursky, Adly Yacoub, Mark Kelley, Walter A. Deutsch, William A. Franklin

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

The Drosophila ribosomal protein S3 has been previously demonstrated to cleave DNA containing 8-oxoguanine residues and has also been found to contain an associated apurinic/apyrimidinic (AP) lyase activity that cleaves phosphodiester bonds via a β, δ-elimination reaction. The activity of this protein on DNA substrates containing incised AP sites was examined. A glutathione S-transferase fusion protein of S3 was found to efficiently remove sugar-phosphate residues from DNA substrates containing 5'-incised AP sites as well as from DNA substrates containing 3'-incised sites. Removal of 2-deoxyribose-5-phosphate as 4-hydroxy-2-pentenal-5-phosphate from a substrate containing 5'-incised AP sites occurred via a β-elimination reaction, as indicated by reaction of the released sugar-phosphate products with sodium thioglycolate. The reaction for the removal of 4-hydroxy-2- pentenal-5-phosphate from the substrate containing 3'-incised AP sites was dependent on the presence of the Mg2+ cation. These findings suggest that the S3 ribosomal protein may function in several steps of the DNA base excision repair pathway in eukaryotes and may represent an important DNA repair function for the repair of oxidative and ionizing radiation-induced DNA damage.

Original languageEnglish
Pages (from-to)17480-17484
Number of pages5
JournalJournal of Biological Chemistry
Volume272
Issue number28
DOIs
StatePublished - 1997

Fingerprint

Drosophila Proteins
DNA
Sugar Phosphates
DNA Repair
Substrates
Repair
Phosphates
Lyases
Ionizing Radiation
Glutathione Transferase
Eukaryota
DNA Damage
Cations
Proteins
Ionizing radiation
ribosomal protein S3
DNA deoxyribophosphodiesterase
Fusion reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity. / Sandigursky, Margarita; Yacoub, Adly; Kelley, Mark; Deutsch, Walter A.; Franklin, William A.

In: Journal of Biological Chemistry, Vol. 272, No. 28, 1997, p. 17480-17484.

Research output: Contribution to journalArticle

Sandigursky, Margarita ; Yacoub, Adly ; Kelley, Mark ; Deutsch, Walter A. ; Franklin, William A. / The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity. In: Journal of Biological Chemistry. 1997 ; Vol. 272, No. 28. pp. 17480-17484.
@article{a5c2b9b00b07450d8b8d44a92d053268,
title = "The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity",
abstract = "The Drosophila ribosomal protein S3 has been previously demonstrated to cleave DNA containing 8-oxoguanine residues and has also been found to contain an associated apurinic/apyrimidinic (AP) lyase activity that cleaves phosphodiester bonds via a β, δ-elimination reaction. The activity of this protein on DNA substrates containing incised AP sites was examined. A glutathione S-transferase fusion protein of S3 was found to efficiently remove sugar-phosphate residues from DNA substrates containing 5'-incised AP sites as well as from DNA substrates containing 3'-incised sites. Removal of 2-deoxyribose-5-phosphate as 4-hydroxy-2-pentenal-5-phosphate from a substrate containing 5'-incised AP sites occurred via a β-elimination reaction, as indicated by reaction of the released sugar-phosphate products with sodium thioglycolate. The reaction for the removal of 4-hydroxy-2- pentenal-5-phosphate from the substrate containing 3'-incised AP sites was dependent on the presence of the Mg2+ cation. These findings suggest that the S3 ribosomal protein may function in several steps of the DNA base excision repair pathway in eukaryotes and may represent an important DNA repair function for the repair of oxidative and ionizing radiation-induced DNA damage.",
author = "Margarita Sandigursky and Adly Yacoub and Mark Kelley and Deutsch, {Walter A.} and Franklin, {William A.}",
year = "1997",
doi = "10.1074/jbc.272.28.17480",
language = "English",
volume = "272",
pages = "17480--17484",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

TY - JOUR

T1 - The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity

AU - Sandigursky, Margarita

AU - Yacoub, Adly

AU - Kelley, Mark

AU - Deutsch, Walter A.

AU - Franklin, William A.

PY - 1997

Y1 - 1997

N2 - The Drosophila ribosomal protein S3 has been previously demonstrated to cleave DNA containing 8-oxoguanine residues and has also been found to contain an associated apurinic/apyrimidinic (AP) lyase activity that cleaves phosphodiester bonds via a β, δ-elimination reaction. The activity of this protein on DNA substrates containing incised AP sites was examined. A glutathione S-transferase fusion protein of S3 was found to efficiently remove sugar-phosphate residues from DNA substrates containing 5'-incised AP sites as well as from DNA substrates containing 3'-incised sites. Removal of 2-deoxyribose-5-phosphate as 4-hydroxy-2-pentenal-5-phosphate from a substrate containing 5'-incised AP sites occurred via a β-elimination reaction, as indicated by reaction of the released sugar-phosphate products with sodium thioglycolate. The reaction for the removal of 4-hydroxy-2- pentenal-5-phosphate from the substrate containing 3'-incised AP sites was dependent on the presence of the Mg2+ cation. These findings suggest that the S3 ribosomal protein may function in several steps of the DNA base excision repair pathway in eukaryotes and may represent an important DNA repair function for the repair of oxidative and ionizing radiation-induced DNA damage.

AB - The Drosophila ribosomal protein S3 has been previously demonstrated to cleave DNA containing 8-oxoguanine residues and has also been found to contain an associated apurinic/apyrimidinic (AP) lyase activity that cleaves phosphodiester bonds via a β, δ-elimination reaction. The activity of this protein on DNA substrates containing incised AP sites was examined. A glutathione S-transferase fusion protein of S3 was found to efficiently remove sugar-phosphate residues from DNA substrates containing 5'-incised AP sites as well as from DNA substrates containing 3'-incised sites. Removal of 2-deoxyribose-5-phosphate as 4-hydroxy-2-pentenal-5-phosphate from a substrate containing 5'-incised AP sites occurred via a β-elimination reaction, as indicated by reaction of the released sugar-phosphate products with sodium thioglycolate. The reaction for the removal of 4-hydroxy-2- pentenal-5-phosphate from the substrate containing 3'-incised AP sites was dependent on the presence of the Mg2+ cation. These findings suggest that the S3 ribosomal protein may function in several steps of the DNA base excision repair pathway in eukaryotes and may represent an important DNA repair function for the repair of oxidative and ionizing radiation-induced DNA damage.

UR - http://www.scopus.com/inward/record.url?scp=0030878398&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030878398&partnerID=8YFLogxK

U2 - 10.1074/jbc.272.28.17480

DO - 10.1074/jbc.272.28.17480

M3 - Article

C2 - 9211893

AN - SCOPUS:0030878398

VL - 272

SP - 17480

EP - 17484

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 28

ER -