rnase h การใช้

• In terms of structure, the replisome is composed of two replicative RNAse H, and ligase.
• Rather RNase H creates a " primer " from the PPT that is resistant to RNase H cleavage.
• Rather RNase H creates a " primer " from the PPT that is resistant to RNase H cleavage.
• Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes.
• In DNA replication, RNase H is responsible for removing the RNA primer, allowing completion of the newly synthesized DNA.
• In addition, boranophosphates have increased nuclease resistance without affecting activation of RNase H cleavage of RNA in RNA : boranophosphate hybrids.
• Thus, RDE-1 s RNase H domain facilitates siRNA maturation but is not directly involved in cleaving target mRNA transcripts.
• RNase H-dependent oligonucleotides cause the target mRNA molecules to be degraded, while steric-blocker oligonucleotides prevent translation of the mRNA molecule.
• The " pol " gene encodes five enzymatic functions : a reverse transcriptase, RNase H, dUTPase, integrase, and protease.
• In addition to the transcription function, retroviral reverse transcriptases have a domain belonging to the RNase H family, which is vital to their replication.
• The antisense oligonucleotides can affect gene expression in two ways : by using an RNase H-dependent mechanism or by using a steric blocking mechanism.
• The 3-D structure of RNase H commonly consists of a 5-stranded ?-sheet surrounded by a distribution of ?-helices.
• Retroviral aspartyl protease is synthesised as part of the POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, RNase H and integrase.
• Within human immunodeficiency virus type 1 ( HIV-1 ), RNase H exists as a domain in the heterodimeric HIV-1 reverse transcriptase enzyme.
• Another target being considered for HIV antivirals include RNase H  which is a component of reverse transcriptase that splits the synthesized DNA from the original viral RNA.
• The majority of antisense drugs function through the RNase H-dependent mechanism, in which RNase H hydrolyzes the RNA strand of the DNA / RNA heteroduplex.
• The majority of antisense drugs function through the RNase H-dependent mechanism, in which RNase H hydrolyzes the RNA strand of the DNA / RNA heteroduplex.
• RNase H plays a role in the priming of the ( + )-strand, but not in the conventional method of synthesizing a new primer sequence.
• The RNA strand is then hydrolyzed by the RNase H domain to enable synthesis of the second DNA strand by the DNA polymerase function of the RT enzyme.
• CaMV contains a circular double-stranded DNA molecule of about 8.0 kilobases, interrupted by nicks that result from the actions of RNAse H during reverse transcription.