Results 31 to 40 of about 14,174,059 (217)
The catalytic mechanism, metal dependence, substrate specificity, and biodiversity of ribonuclease H
Ribonucleoside monophosphates are inevitably misincorporated into the DNA genome inside cells, and they need to be excised to avoid chromosome instability.
Jing Pang, Qinyu Guo, Zheng Lu
doaj +1 more source
HIV-1 RT-Associated RNase H review
HIV-RT is an essential enzyme for HIV replication it comprises two associated functions: RNA- and DNA-dependent DNA polymerase (RDDP & DDDP) and ribonuclease H (RNase H).
Madonna M. A. Mitry+2 more
doaj +1 more source
Insights into the structure and activity of prototype foamy virus RNase H
Background RNase H is an endonuclease that hydrolyzes the RNA strand in RNA/DNA hybrids. Retroviral reverse transcriptases harbor a C-terminal RNase H domain whose activity is essential for viral replication.
Leo Berit+4 more
doaj +1 more source
The persistence of the AIDS epidemic, and the life-long treatment required, indicate the constant need of novel HIV-1 inhibitors. In this scenario the HIV-1 Reverse Transcriptase (RT)-associated ribonuclease H (RNase H) function is a promising drug ...
Angela Corona+5 more
doaj +1 more source
Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes
Background A theoretical model of genetic redundancy has proposed that the fates of redundant genes depend on the degree of functional redundancy, and that functionally redundant genes will not be inherited together.
Tomita Masaru+2 more
doaj +1 more source
Ribonuclease H/DNA Polymerase HIV-1 Reverse Transcriptase Dual Inhibitor: Mechanistic Studies on the Allosteric Mode of Action of Isatin-Based Compound RMNC6. [PDF]
The DNA polymerase and ribonuclease H (RNase H) activities of human immunodeficiency virus type 1 (HIV-1) are needed for the replication of the viral genome and are validated drug targets.
Angela Corona+10 more
doaj +1 more source
The Unfolding Behavior of RNase H Under Force [PDF]
We have used optical tweezers to revisit the energy landscape of E. coli RNase H under mechanical force. This protein's equilibrium energetics and folding pathway have been studied in bulk and in single-molecule mechanical denaturation experiments, which showed the presence of a collapsed folding intermediate that is on-pathway to the native state (1 ...
Susan Marqusee+2 more
openaire +2 more sources
RNase H enables efficient repair of R-loop induced DNA damage
R-loops, three-stranded structures that form when transcripts hybridize to chromosomal DNA, are potent agents of genome instability. This instability has been explained by the ability of R-loops to induce DNA damage. Here, we show that persistent R-loops
J. Amon, D. Koshland
semanticscholar +1 more source
Escherichia coli RNase H has a basic extension that is involved in binding nucleic acid substrates. This basic extension is present in the RNase H of Moloney murine leukemia virus reverse transcriptase (MLV RT), but has been deleted from the RNase H of HIV-1 RT. Previous work showed that removing the basic loop from MLV RT (the mutant is called DeltaC)
Stephen H. Hughes+4 more
openaire +3 more sources
Selective inhibition of RNase H by dextran.
Ordinarily, ribonuclease H hydrolyzes poly(rA) . poly(dT) and phiX174DNA-RNA at equal rates. Here we show that in the presence of dextran, the degradation of poly(rA) . poly(dT) is inhibited, while that of phi 174DNA-RNA is not. A similar inhibition by sucrose is found to be due to trace contamination of dextran in the sucrose. Ribose, deoxyribose, and
M L Dirksen, R J Crouch
openaire +3 more sources