Results 291 to 300 of about 476,060 (306)

Improvement of Reverse Transcription PCR by RNase H

Bioscience, Biotechnology, and Biochemistry, 2003
An improvement in the method of the Reverse Transcription PCR (RT-PCR) using RNase H is proposed here. We succeeded in RT-PCR amplification against the full sequence of the coding region (8.9 kb) of the Insulin-like growth factor II receptor gene which has the area called the GC-block of about 90% GC contents at the 5' terminal.
Muneharu Esaka, Masao Kitabayashi
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RNase H-defective mutants of Escherichia coli: A possible discriminatory role of RNase H in initiation of DNA replication

Molecular and General Genetics MGG, 1984
Mutants of Escherichia coli completely deficient in RNase H activity were isolated by inserting transposon Tn3 into the structural gene for RNase H, rnh, and its promoter. These rnh- mutants exhibited the following phenotypes; (1) the mutants grew fairly normally, (2) rnh- cells could be transformed with ColE1 derivative plasmids, pBR322 and pML21 ...
Takashi Horiuchi, Mutsuo Sekiguchi, Hisaji Maki   +2 more
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Structure and Function of RNase H Enzymes

2011
RNase H enzymes are endonucleases that specifically cleave ribonucleotides within an RNA:DNA duplex. RNase H proteins are divided into type 1 and type 2 enzymes based on amino acid sequence similarities, substrate specificity, and structure. Both RNase H1 and RNase H2 enzymes play important roles in DNA replication, repair and transcription, and at ...
Thomas Hollis, Nadine M. Shaban
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Chemically modified oligonucleotides with efficient RNase H response

Bioorganic & Medicinal Chemistry Letters, 2008
Ten different chemically modified nucleosides were incorporated into short DNA strands (chimeric oligonucleotides ON3-ON12 and ON15-ON24) and then tested for their capacity to mediate RNAse H cleavage of the complementary RNA strand. The modifications were placed at two central positions directly in the RNase H cleaving region.
Sune Lobedanz, Pawan K. Sharma, Pawan K. Sharma, Jesper Wengel, Michael Raunkjær, Raunak, Surender Kumar, Birte Vester, Poul Nielsen, B. Ravindra Babu, Anne Marie Boel, Torben Højland, Dorthe Lindegaard, Patrick J. Hrdlicka   +13 more
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A large deletion in the connection subdomain of murine leukemia virus reverse transcriptase or replacement of the RNase H domain with Escherichia coli RNase H results in altered polymerase and RNase H activities

Biochemistry, 1993
The functional relationship between the polymerase and RNase H domains of reverse transcriptase (RT) was investigated by studying the activities of AKR murine leukemia virus (MuLV) enzymes. In addition to the wild type, an RNase H-minus RT missing the entire RNase H domain and two other mutants having abnormal polymerase:RNase H ratios were expressed ...
Tsuneko Uchida, Jianhui Guo, Judith G. Levin, Eva Kalman, Klara Post, Robert J. Crouch   +5 more
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Mammalian retrovirus-associated RNase H is virus coded

Journal of Virology, 1978
RNase H of a temperature-sensitive mutant of Rauscher murine leukemia virus is thermolabile, establishing this activity as a virus-coded function of the mammalian type C virus reverse transcriptase.
M H Lai, Steven R. Tronick, Stuart A. Aaronson, I M Verma   +3 more
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Molecular Cloning and Expression of cDNA for Human RNase H

Antisense and Nucleic Acid Drug Development, 1998
We have cloned, expressed, and purified to electrophoretic homogeneity a human RNase H. The enzyme has a molecular weight of 32 kDa, is Mg2+ dependent, and is inhibited by Mn2+ and N-ethylmaleimide. Its molecular weight and cleavage characteristics are consistent with type 2 human RNase H.
Hongjiang Wu, Stanley T. Crooke, Walt F. Lima   +2 more
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Association of RNase H activity with yeast RNA polymerase A

Nature, 1976
EUKARYOTIC RNA polymerases were isolated as large multimeric protein complexes containing two high molecular weight subunits and a collection of smaller polypeptide chains1–3. This structural complexity suggests a multifunctional system, organised around a core enzyme combined with specificity determinants and possibly other proteins involved in ...
Françoise Wyers, Jean-Marie Buhler, Janine Huet, Pierre Fromageot, André Sentenac   +4 more
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Recognition of Internal Cleavage Sites by Retroviral RNases H

Journal of Molecular Biology, 2004
The RNase H activity of reverse transcriptase is essential to complete retroviral replication. Many studies have characterized how reverse transcriptase associates with recessed and exposed DNA 3' ends or RNA 5' ends to position the RNase H domain for cleavage, but little is known about how a nick might affect RNase H cleavages, or how RNase H carries ...
James J. Champoux, Miaohua Zhang, Sharon J. Schultz   +2 more
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The RNase H Domain: Structure, Function and Mechanism

2013
An essential step of proliferation of retroviruses and transposition of long terminal repeat-containing retrotransposons is conversion of their single-stranded RNA genome into integration-competent, double-stranded proviral DNA by the multifunctional reverse transcriptase (RT) (Gilboa et al. 1979). RT is an enzyme with two activities. RNA-dependent DNA
Marcin Nowotny, Małgorzata Figiel
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