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Related Concept Videos

Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
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The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
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Position-effect Variegation02:32

Position-effect Variegation

In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
Homologous Recombination02:31

Homologous Recombination

The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Sequence context effect for hMSH2-hMSH6 mismatch-dependent activation.

Anthony Mazurek1, Christopher N Johnson, Markus W Germann

  • 1Department of Molecular Virology, Immunology, and Medical Genetics, Ohio State University Medical Center, 400 West 12th Avenue, Columbus, OH 43210, USA.

Proceedings of the National Academy of Sciences of the United States of America
|February 25, 2009
PubMed
Summary
This summary is machine-generated.

DNA sequence context significantly impacts MutS homologue (MSH) ATPase activity, crucial for DNA mismatch repair (MMR). Symmetric 3'-purines enhance MSH activation, while 3'-pyrimidines reduce it, linked to DNA flexibility.

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Published on: September 23, 2011

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • MutS homologue (MSH) ATPase activity is vital for DNA mismatch repair (MMR).
  • Sequence context surrounding DNA mismatches influences MSH protein function.
  • Understanding these interactions is key to deciphering MMR pathway regulation.

Purpose of the Study:

  • To investigate how specific DNA sequence contexts affect hMSH2-hMSH6 ATPase activation.
  • To determine the relationship between sequence context, mismatch binding, and DNA flexibility.
  • To elucidate the molecular mechanisms underlying MSH-mediated DNA repair activation.

Main Methods:

  • In vitro assays measuring hMSH2-hMSH6 ATPase activity.
  • DNA binding affinity (K(D)) and oligonucleotide melting temperature (T(m)) measurements.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to assess DNA dynamics (imino proton lifetime, solvent accessibility, NOE connectivity).

Main Results:

  • Symmetric 3'-purine contexts enhanced hMSH2-hMSH6 ATPase activation, while symmetric 3'-pyrimidine contexts reduced it.
  • This sequence context effect was most pronounced for G-containing mispairs.
  • Enhanced ATPase activation correlated with increased localized DNA flexibility, identified through NMR, but not solely with binding affinity or melting parameters.

Conclusions:

  • DNA sequence context, particularly the presence of 3'-purines or pyrimidines, modulates MSH ATPase activity and DNA mismatch repair.
  • Localized DNA flexibility appears to be a critical determinant of MSH activation efficiency.
  • This dynamic DNA signature may explain the broad substrate specificity of MSH proteins in recognizing diverse DNA lesions.