A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG

Yvette Habraken, Patrick Sung, Louise Prakash, Satya Prakash

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Saccharomyces cerevisiae RAD2 protein and its human homolog xeroderma pigmentosum group G (XPG) protein function in the incision step of nucleotide excision repair of DNA damaged by ultraviolet light. Both RAD2 and XPG proteins have been shown previously to possess an endonuclease activity. Using DNA substrates labeled at either the 5′ end or 3′ end, we now demonstrate that RAD2 protein also digests both single-stranded and double-stranded DNAs exonucleolytically with a 5′ to 3′ directionality. A 5′ to 3′ exonuclease activity is also present in the XPG protein, indicating evolutionary conservation of this activity. The possible role of RAD2 and XPG 5′ to 3′ exonuclease activity in nucleotide excision repair is discussed.

Original languageEnglish (US)
Pages (from-to)31342-31345
Number of pages4
JournalJournal of Biological Chemistry
Volume269
Issue number50
StatePublished - Dec 16 1994

Fingerprint

spleen exonuclease
Xeroderma Pigmentosum
Exonucleases
GTP-Binding Proteins
DNA Repair
Yeast
Repair
Nucleotides
Yeasts
DNA
Proteins
Endonucleases
Saccharomyces cerevisiae Proteins
Conservation
Ultraviolet Rays
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG. / Habraken, Yvette; Sung, Patrick; Prakash, Louise; Prakash, Satya.

In: Journal of Biological Chemistry, Vol. 269, No. 50, 16.12.1994, p. 31342-31345.

Research output: Contribution to journalArticle

@article{4c5a110fa0154608b299fc1bf9a81bc8,
title = "A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG",
abstract = "Saccharomyces cerevisiae RAD2 protein and its human homolog xeroderma pigmentosum group G (XPG) protein function in the incision step of nucleotide excision repair of DNA damaged by ultraviolet light. Both RAD2 and XPG proteins have been shown previously to possess an endonuclease activity. Using DNA substrates labeled at either the 5′ end or 3′ end, we now demonstrate that RAD2 protein also digests both single-stranded and double-stranded DNAs exonucleolytically with a 5′ to 3′ directionality. A 5′ to 3′ exonuclease activity is also present in the XPG protein, indicating evolutionary conservation of this activity. The possible role of RAD2 and XPG 5′ to 3′ exonuclease activity in nucleotide excision repair is discussed.",
author = "Yvette Habraken and Patrick Sung and Louise Prakash and Satya Prakash",
year = "1994",
month = "12",
day = "16",
language = "English (US)",
volume = "269",
pages = "31342--31345",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "50",

}

TY - JOUR

T1 - A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG

AU - Habraken, Yvette

AU - Sung, Patrick

AU - Prakash, Louise

AU - Prakash, Satya

PY - 1994/12/16

Y1 - 1994/12/16

N2 - Saccharomyces cerevisiae RAD2 protein and its human homolog xeroderma pigmentosum group G (XPG) protein function in the incision step of nucleotide excision repair of DNA damaged by ultraviolet light. Both RAD2 and XPG proteins have been shown previously to possess an endonuclease activity. Using DNA substrates labeled at either the 5′ end or 3′ end, we now demonstrate that RAD2 protein also digests both single-stranded and double-stranded DNAs exonucleolytically with a 5′ to 3′ directionality. A 5′ to 3′ exonuclease activity is also present in the XPG protein, indicating evolutionary conservation of this activity. The possible role of RAD2 and XPG 5′ to 3′ exonuclease activity in nucleotide excision repair is discussed.

AB - Saccharomyces cerevisiae RAD2 protein and its human homolog xeroderma pigmentosum group G (XPG) protein function in the incision step of nucleotide excision repair of DNA damaged by ultraviolet light. Both RAD2 and XPG proteins have been shown previously to possess an endonuclease activity. Using DNA substrates labeled at either the 5′ end or 3′ end, we now demonstrate that RAD2 protein also digests both single-stranded and double-stranded DNAs exonucleolytically with a 5′ to 3′ directionality. A 5′ to 3′ exonuclease activity is also present in the XPG protein, indicating evolutionary conservation of this activity. The possible role of RAD2 and XPG 5′ to 3′ exonuclease activity in nucleotide excision repair is discussed.

UR - http://www.scopus.com/inward/record.url?scp=0028075835&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028075835&partnerID=8YFLogxK

M3 - Article

VL - 269

SP - 31342

EP - 31345

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 50

ER -