WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups.

WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Research Abstract Details 

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WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Abstract Text:

Jeanine A Harrigan,Jinshui Fan,Jamil Momand,Fred W Perrino,Vilhelm A Bohr,David M Wilson,

Reactive oxygen species, generated either by cellular respiration or upon exposure to environmental agents such as ionizing radiation (IR), attack DNA to form a variety of oxidized base and sugar modifications. Accumulation of oxidative DNA damage has been associated with age-related disease as well as the aging process. Single-strand breaks harboring oxidative 3' obstructive termini, e.g. 3' phosphates and 3' phosphoglycolates, must be removed prior to DNA repair synthesis or ligation. In addition, 3' tyrosyl-linked protein damage, resulting from therapeutic agents such as camptothecin (CPT), must be processed to initiate repair. Several nucleases participate in DNA repair and the excision of 3' obstructive ends. As the protein defective in the segmental progeroid Werner syndrome (WRN) possesses 3'-5' exonuclease activity, and Werner syndrome cells are hypersensitive to IR and CPT, we examined for WRN exonuclease activity on 3' blocking lesions. Moreover, we compared side-by-side the activity of four prominent human 3'-5' exonucleases (WRN, APE1, TREX1, and p53) on substrates containing 3' phosphates, phosphoglycolates, and tyrosyl residues. Our studies reveal that while WRN degrades 3' hydroxyl containing substrates in a non-processive manner, it does not excise 3' phosphate, phosphoglycolate, or tyrosyl groups. In addition, we found that APE1 was most active at excising 3' blocking termini in comparison to the disease-related exonucleases TREX1, WRN, and p53 under identical physiological reaction conditions, and that TREX1 was the most powerful 3'-5' exonuclease on undamaged oligonucleotide substrates.

WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Publishing Authors By Initials

JA Harrigan,J Fan,J Momand,FW Perrino,VA Bohr,DM Wilson,

For similar amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research

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MEDLINE DATE:

WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Intr

Journal: Mechanisms of ageing and development

VOLUME: 128

Page Numbers: 259-66

Journal Abbreviation: Mech. Ageing Dev.

ISSN: 0047-6374

DAY: 20

MONTH: 12

YEAR: 2006

WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 347227

WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Keywords Mesh Terms:

KEYWORDS: Tyrosine

MESH TERMS: chemistry

Chemical & Substance for Abstract: WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups. Information

Substance Name: DNA-(Apurinic or Apyrimidinic Site) Lyas

Registry Number: EC 4.2.99.18

Grant and Affiliation Information for WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups.

AFFILIATION: Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, United States.

Country: Ireland

AGENCY: United States NIGMS

GRANT: GM069962

ACRONYM: GM

MEDLINETA: Mech Ageing Dev

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