Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity

Article Abstract:

The structure and activity of the Pyrococcus furiosus's flap endonuclease 1 (FEN-1) were studied to determine its role in DNA repair and replication. The crystal structure of FEN-1 exhibited interactions for the single- and double-stranded portions of the flap DNA substrate. The binding of the flap DNA substrates' stranded regions were influenced by two structural motifs. It was revealed that the conserved C terminus of FEN-1 influenced its involvement in the DNA replication fork apparatus through the interaction with the C-terminal face of the proliferating cell nuclear antigen.

Author: Mol, Clifford D., Tainer, John A., Hosfield, David J., Shen, Binghui
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Bacteria, Thermophilic, Thermophiles

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis

Article Abstract:

A study was conducted to determine the atomic structure of Escherichia coli endonuclease IV both alone and in complex with duplex DNA containing a synthetic abasic site. Results provide information on the structures of the Endo IV apurinic/apyrimidinic enduclease family and the DNA-bound structures for a DNA repair enzyme. These structures reveal a new use of alpha8beta8 TIM barrel fold for DNA binding and identify key structural features responsible for DNA damage recognition and catalysis.

Author: Hosfield, David J., Guan, Yue, Haas, Brian J., Cunnigham, Richard P., TAiner, John A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
Escherichia coli, Catalysis, Atomic structure

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair

Article Abstract:

Flap EndoNuclease-1 (FEN-1) is a structure-specific nuclease that is central to both DNA replication and repair processes. The DNA and protein conformational changes, composite complex structures, FRET, and mutational results support enzyme-PCNA (proliferating cell nuclear anti-clamp) alignments are discussed.

Author: Chapados, Brian R., Hosfield, David J., Han, Seungil, Qiu, Junzhuan, Yelent, Biana ; Shen, Binghui ; Tainer, John A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
Science & research, Proteins, Genetic research, DNA replication

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, DNA repair, Restriction enzymes, DNA, DNA restriction enzymes
Similar abstracts:
  • Abstracts: Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53
  • Abstracts: Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53. part 2
  • Abstracts: Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase
  • Abstracts: Effects of growth medium, inoculum size, and incubation time on culturability and isolation of soil bacteria
  • Abstracts: mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability. What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2026 Advameg, Inc.