A Human PMS2 Homologue from Aquifex aeolicus Stimulates an ATP-dependent DNA Helicase
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منابع مشابه
(TrmD) from Aquifex aeolicus
Genes to Cells (2006) 11 , 1353–1365 Journal compilation © 2006 by the Molecular Biology Society of Japan/Blackwell Publishing Ltd. 1353 DOI: 10.1111/j.1365-2443.2006.01022.x Blackwell Publishing Inc M lden, USA GTC enes to Cells 1356-9597 © Blackwell Publ shing Ltd ? 2006 1 Original Artic e tRNA specificity of Aquifex aeolicus TrmD H. Takeda e al. The substrate specificity of tRNA (m 1 G37) me...
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An NAD(+)-dependent DNA ligase from the hyperthermophilic bacterium Aquifex aeolicus was cloned, expressed in Escherichia coli and purified to homogeneity. The enzyme is most active in slightly alkaline pH conditions with either Mg(2+)or Mn(2+)as the metal cofactor. Ca(2+)and Ni(2+)mainly support formation of DNA-adenylate intermediates. The catalytic cycle is characterized by a low k (cat)valu...
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BACKGROUND Human PMS2 (hPMS2) homologues act to nick 5' and 3' to misincorporated nucleotides during mismatch repair in organisms that lack MutH. Mn(++) was previously found to stimulate the endonuclease activity of these homologues. ATP was required for the nicking activity of hPMS2 and yPMS1, but was reported to inhibit bacterial MutL proteins from Thermus thermophilus and Aquifex aeolicus th...
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Differential effects of replacing Escherichia coli ribosomal protein L27 with its homologue from Aquifex aeolicus.
The rpmA gene, which encodes 50S ribosomal subunit protein L27, was cloned from the extreme thermophile Aquifex aeolicus, and the protein was overexpressed and purified. Comparison of the A. aeolicus protein with its homologue from Escherichia coli by circular dichroism analysis and proton nuclear magnetic resonance spectroscopy showed that it readily adopts some structure in solution that is v...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m109.050955