Sentences with phrase «of ribonuclease»

Analysis of crosslinked complexes of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli, and transfer RNA precursor substrates has led to the identification of regions in the enzyme and in the substrate that are in close physical proximity to each other.

The picture that emerges from the work is of ribonucleases patrolling our bodies, looking for telltales of cancer cells, Raines says.

Areas of emphasis include the roles of ribonucleases and RNA - binding proteins and assembly of the carbon - fixing enzyme Rubisco.

Not exact matches

Standard laboratory DNA isolation methods, such as sonication, ribonuclease (RNase) treatment, and ethanol precipitation may reduce the available pool of DNA enough to prevent recovering usable sequences from the oldest samples.

The most efficient EGSs form transfer RNA precursor - like structures with the target RNA, in which the analog of the anticodon stem has been disrupted, an indication that selection for the optimal substrate for ribonuclease P yields an RNA structure different from that of present - day transfer RNA precursors.

Any RNA, when in a complex with another oligoribonucleotide known as an external guide sequence (EGS), can become a substrate for ribonuclease P. Simulation of evolution in vitro was used to select EGSs that bind tightly to a target substrate messenger RNA and that increase the efficiency of cleavage of the target by human ribonuclease P to a level equal to that achieved with natural substrates.

Ribonuclease P (RNase P) from Escherichia coli or its catalytic RNA subunit can efficiently cleave small RNA substrates that lack the conserved features of natural substrates of RNase P if an additional small RNA is also present.

M1 RNA, the catalytic RNA subunit of Escherichia coli ribonuclease P, can cleave novel transfer RNA (tRNA) precursors that lack specific domains of the normal tRNA sequence.

Bernstein et al. «Role for A Bidentate Ribonuclease in the Initiation Step of RNA Interference», Nature, 409: 363 - 366, 2001.

Crystal structures of the reverse transcriptase - associated ribonuclease H domain of xenotropic murine leukemia - virus related virus

A fluorescence - based high - throughput screening assay for inhibitors of human immunodeficiency virus - 1 reverse transcriptase - associated ribonuclease H activity