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Related Experiment Videos

Alkyltransferase-like proteins.

Geoffrey P Margison1, Amna Butt, Steven J Pearson

  • 1Cancer Research-UK Carcinogenesis Group, Paterson Institute for Cancer Research, University of Manchester, Manchester M20 4BX, United Kingdom. gmargison@picr.man.ac.uk

DNA Repair
|May 15, 2007
PubMed
Summary
This summary is machine-generated.

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Alkyltransferase-like (ATL) proteins bind to DNA damage but do not repair it. These proteins likely protect organisms from alkylating agents by signaling DNA lesions for other repair pathways.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Proteins with sequence similarity to O(6)-alkylguanine-DNA alkyltransferases (AGTs) exist in prokaryotes and lower eukaryotes, but not humans.
  • These proteins, termed alkyltransferase-like (ATL) proteins, have a residue other than cysteine at the putative active site.

Purpose of the Study:

  • To review recent work on ATL proteins.
  • To consider their mechanism of action, role in protecting host organisms against O(6)-alkylating agents, and evolution.

Main Methods:

  • In silico analysis to identify ATL proteins.
  • Biochemical assays to determine the activity of purified ATL proteins (e.g., E. coli eAtl, S. pombe Atl1).
  • Genetic analysis of S. pombe atl1 inactivation.

Related Experiment Videos

Main Results:

  • ATL proteins bind to O(6)-alkylguanine DNA lesions.
  • ATL proteins inhibit human AGT (MGMT) activity on these lesions.
  • ATL proteins lack DNA repair activity (methyl removal, glycosylase, endonuclease).
  • S. pombe lacking functional AGT is sensitive to alkylating agents, and Atl1 inactivation exacerbates this sensitivity.

Conclusions:

  • ATL proteins likely function by binding to O(6)-alkylguanine lesions and signaling them for repair by other pathways.
  • The findings suggest a conserved role for ATL proteins in DNA damage response across different organisms.
  • The evolutionary origin of ATL proteins may involve independent mutations in AGT genes.