Results 301 to 310 of about 19,244,439 (340)

An RNase H-Like gene complements resistance to Bean common mosaic necrosis virus in Phaseolus vulgaris. [PDF]

Plant Genome
Soler-Garzón A, Miklas PN.
europepmc   +1 more source

The Potential Impact of Edible Fruit Extracts on Bacterial Nucleases in Preliminary Research-In Silico and In Vitro Insight. [PDF]

Int J Mol Sci
Szeleszczuk Ł, Brożyna M, Dudek B, Czarnecki M, Junka A, Czerwińska ME.   +5 more
europepmc   +1 more source

Regulation of plant gene expression by tsRNAs in response to abiotic stress. [PDF]

PeerJ
Li C, Zhu J, Jin H, Feng H, Zhuang H, Du Z, Zhu G, He H, Ye F, Mo Z, Hu Q, Chen Z, Liu K, Wan X.   +13 more
europepmc   +1 more source

Recent studies of ribonuclease P. [PDF]

The FASEB Journal, 1993
RNase P is an essential enzyme that is required for the biosynthesis of tRNA. It is composed of RNA and protein subunits. The RNA subunit of the enzyme derived from eubacterial sources can carry out the catalytic function by itself in vitro. Current studies of RNase P focus on structure-function relationships with respect to interactions of the RNA ...
Leif A. Kirsebom, Sidney Altman, Simon J. Talbot   +2 more
openaire   +2 more sources

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The varieties of ribonuclease P

Trends in Biochemical Sciences, 1992
Ribonuclease P is a ribozyme involved in tRNA processing that is present in all cells and organelles that synthesize tRNA. Most of our understanding of ribonuclease P derives from studies of the bacterial enzyme. This enzyme has been characterized biochemically and a secondary structure for the RNA subunit has been proposed.
Sylvia C. Darr, Norman R. Pace, James W. Brown   +2 more
openaire   +3 more sources

The enigma of ribonuclease P evolution

Trends in Genetics, 2003
The 5'-end maturation of tRNAs is catalyzed by the ribonucleoprotein enzyme ribonuclease P (RNase P) in all organisms. Here we provide, for the first time, a comprehensive overview on the representation of individual RNase P protein homologs within the Eukarya and Archaea.
Roland K. Hartmann, Enno Hartmann
openaire   +2 more sources

Ribonuclease P: a ribonucleoprotein enzyme

Current Opinion in Chemical Biology, 2000
The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5' end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA-P-protein and RNase-P-RNA-precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the ...
Jeffrey C. Kurz, Carol A. Fierke
openaire   +3 more sources

Human Ribonuclease P

2001
Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
Nayef Jarrous, Sidney Altman
openaire   +3 more sources

Determination of the Specificity Landscape for Ribonuclease P Processing of Precursor tRNA 5' Leader Sequences.

ACS Chemical Biology, 2016
Maturation of tRNA depends on a single endonuclease, ribonuclease P (RNase P), to remove highly variable 5' leader sequences from precursor tRNA transcripts. Here, we use high-throughput enzymology to report multiple-turnover and single-turnover kinetics
C. Niland, J. Zhao, Hsuan-Chun Lin, David R Anderson, E. Jankowsky, M. Harris   +5 more
semanticscholar   +1 more source

Modifications of ribonuclease A induced by p-benzoquinone

Bioorganic Chemistry, 2012
The nature of ribonuclease A (RNase) modifications induced by p-benzoquinone (pBQ) was investigated using several analysis methods. SDS-PAGE experiments revealed that pBQ was efficient in producing oligomers and polymeric aggregates when RNase was incubated with pBQ.
Albert R. Vaughn, Chris Cho, Jisook Kim, Ethan A. Carver, Titus V. Albu   +4 more
openaire   +3 more sources