Results 321 to 330 of about 19,244,439 (340)

Purification and characterization of potato ribonuclease P

Journal of Plant Biochemistry and Biotechnology, 2012
Ribonuclease P (RNase P), a ribonucleo-protein endoribonuclease, responsible for 5′ maturation of precursor tDNA, is well characterized in bacteria, yeast and human, but not in plant. Attempt has been made to partially purify and characterize nuclear RNase P from potato.
Duni Chand, Anupama Singh, Debasis Pattanayak   +2 more
openaire   +2 more sources

Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli.

Biochemistry, 1986
M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli, can under certain conditions catalytically cleave precursors to tRNA in the absence of C5, the protein moiety of RNase P.
C. Guerrier-Takada, K. Haydock, L. C. Allen, S. Altman   +3 more
semanticscholar   +1 more source

Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme.

Science, 1988
The Bacillus subtilis ribonuclease P consists of a protein and an RNA. At high ionic strength the reaction is protein-independent; the RNA alone is capable of cleaving precursor transfer RNA, but the turnover is slow. Kinetic analyses show that high salt
Claudia I. Reich, Gary J. Olsen, Bernadette Pace, Norman R. Pace   +3 more
semanticscholar   +1 more source

Ribonuclease P as a Tool

2009
Two gene-targeting approaches have been developed with the use of RNase P. The first approach is based on an external guide sequence (EGS), which consists of a sequence complementary to a target mRNA and, when noncovalently complexed with RNase P, renders the target RNA susceptible to degradation by the ribonuclease.
openaire   +2 more sources

Crystal structure of the specificity domain of ribonuclease P

Nature, 2003
RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo ...
Andrey S. Krasilnikov, Tao Pan, Alfonso Mondragón, Xiaojing Yang   +3 more
openaire   +3 more sources

Long-Range Structure in Ribonuclease P RNA

Science, 1991
Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA.
James W. Brown, Norman R. Pace, Daniel P. Morse, Elizabeth S. Haas, Francis J. Schmidt   +4 more
openaire   +3 more sources

A Structural Analysis of Ribonuclease P

2007
The endonucleolytic cleavage of precursor sequences from the 5′-end of transfer RNA (tRNA) precursors to form the mature 5′-end is catalyzed by a remarkably complex and unusual enzyme, ribonuclease P (RNase P)(Figure 9.1).1–4 RNase P is ubiquitous, found in cells from all three domains of life: Bact...
Norman R. Pace, Steven M. Marquez, Alexei V. Kazantsev, Donald Evans   +3 more
openaire   +2 more sources

Characterization of ribonuclease P from Toxoplasma gondii

European Journal of Protistology, 1996
Summary Toxoplasma gondii ribonuclease P (RNase P) activity was identified and characterized. The enzyme cleaved the precursor of Escherichia coli tyrosine transfer RNA at a position identical to the site recognized by E. coli RNase P. The enzyme has a broad pH optimum from 7 to 9, is more active at 42°C than at 32°C and 37°C, and is relatively
Douglas G. Mack, Douglas G. Mack, Rima McLeod, Rima McLeod, Benjamin C. Stark   +4 more
openaire   +3 more sources

Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21.

Biochemistry, 2005
Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the removal of 5' leader sequences from tRNA precursors (pre-tRNA). The human protein Rpp21 is essential for human RNase P activity in tRNA processing in vitro.
Y. Kakuta, Ikuko Ishimatsu, T. Numata, K. Kimura, M. Yao, I. Tanaka, M. Kimura   +6 more
semanticscholar   +1 more source

Ribonucleoprotein Ribonucleases P and MRP

2011
Ribonucleoprotein Ribonuclease (RNase) P and RNase MRP consist of a large RNA component and an essential protein part. RNases P/MRP differ from all other known ribonucleases in that it is their RNA component, not protein that is responsible for the endonucleolytic cleavage of substrates.
openaire   +2 more sources