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PMID: 11413147 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Involvement of the nucleotide excision repair protein UvrA in instability of CAG*CTG repeat sequences in Escherichia coli.

The Journal of biological chemistry ·Vol. 276 ·No. 33 ·2001-08-17 ·Pages 30878-84

Oussatcheva EA, Hashem VI, Zou Y, Sinden RR, Potaman VN

Abstract

Several human genetic diseases have been associated with the genetic instability, specifically expansion, of trinucleotide repeat sequences such as (CTG)(n).(CAG)(n). Molecular models of repeat instability imply replication slippage and the formation of loops and imperfect hairpins in single strands. Subsequently, these loops or hairpins may be recognized and processed by DNA repair systems. To evaluate the potential role of nucleotide excision repair in repeat instability, we measured the rates of repeat deletion in wild type and excision repair-deficient Escherichia coli strains (using a genetic assay for deletions). The rate of triplet repeat deletion decreased in an E. coli strain deficient in the damage recognition protein UvrA. Moreover, loops containing 23 CTG repeats were less efficiently excised from heteroduplex plasmids after their transformation into the uvrA(-) strain. As a result, an increased proportion of plasmids containing the full-length repeat were recovered after the replication of heteroduplex plasmids containing unrepaired loops. In biochemical experiments, UvrA bound to heteroduplex substrates containing repeat loops of 1, 2, or 17 CAG repeats with a K(d) of about 10-20 nm, which is an affinity about 2 orders of magnitude higher than that of UvrA bound to the control substrates containing (CTG)(n).(CAG)(n) in the linear form. These results suggest that UvrA is involved in triplet repeat instability in cells. Specifically, UvrA may bind to loops formed during replication slippage or in slipped strand DNA and initiate DNA repair events that result in repeat deletion. These results imply a more comprehensive role for UvrA, in addition to the recognition of DNA damage, in maintaining the integrity of the genome.

MeSH Terms
Adenosine Triphosphatases/physiology Bacterial Proteins/physiology DNA Repair DNA, Bacterial/chemistry DNA-Binding Proteins/physiology Escherichia coli/genetics Escherichia coli Proteins Nucleic Acid Heteroduplexes/metabolism Plasmids Trinucleotide Repeats
Chemicals
Bacterial Proteins DNA, Bacterial DNA-Binding Proteins Escherichia coli Proteins Nucleic Acid Heteroduplexes UvrA protein, E coli Adenosine Triphosphatases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Oussatcheva E A
Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, Texas 77030, USA.
Hashem V I
Zou Y
Sinden R R
Potaman V N
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2001-08-17
Epub
2001-00-18
Pages
30878-84
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIEHS NIH HHS · ES05508 · United States
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