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Modular organization of RNase P [PDF]

open access: possible, 2008
Ribonuclease P (RNase P) is a ribozyme that removes the 5′ precursor sequence from premature t-RNAs. In bacteria this complex consists of one RNA subunit and a single protein subunit, whereas in eukaryotes one RNA subunit and nine protein subunits contribute. We have determined the structure of eukaryotic RNase P at ca. 15 ?
Bettina Böttcher   +2 more
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Plant mitochondrial RNase P

Molecular Biology Reports, 1996
Molecular investigations in mitochondria of higher plants have to take in account the complicated genomic structure of these organelles and their complex mode of gene expression. Recently tRNA processing activities and particularly RNase P-like activities have been described for mitochondria of mono- and dicot plants.
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The RNase P ofDictostyelium discoideum

Molecular Biology Reports, 1996
Ribonuclease P (RNase P) is a key enzyme involved in tRNA biosynthesis. It catalyses the endonucleolytic cleavage of nearly all tRNA precursors to produce 5'-end matured tRNA. RNase P activity has been found in all organisms examined, from bacteria to mammals.
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RNase P RNA-mediated catalysis [PDF]

open access: possibleBiochemical Society Transactions, 2002
The endoribonuclease RNase P is involved in the processing of tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P is associated with an RNA, RNase P RNA. A specific interaction between the 3′ end of the substrate and RNase P RNA, to form an RNase P RNA-substrate complex, is referred to as the ‘73–294-interaction’.
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Diversity and Evolution of RNase P

2020
Ribonuclease P (RNase P) is the essential endonuclease responsible for the 5’-end maturation of tRNAs. It is found in all forms of life, yet in an unprecedented variety of architectures. RNase P enzymes are, on the one hand, represented by RNA-based forms, where a structurally conserved, catalytic RNA molecule is associated with one or more (up to ten ...
Walter Rossmanith   +2 more
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RNase P RNA ofMycoplasma capricolum

Molecular Biology Reports, 1996
There are at least six small stable RNAs in Mycoplasma capricolum cells besides tRNAs and rRNAs. One of them, MCS5 RNA, is a homolog of RNase P RNA. The predicted secondary structure of this RNA is essentially the same as that of other eubacterial RNase P RNAs. MCS5 RNA is more similar to the RNase P RNA of B. Subtilis than to that of E. coli.
Dai Izawa, Chisato Ushida, Akira Muto
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Yeast mitochondrial RNase P: an unusual member of the RNase P enzyme family

1995
We review here our studies of the tRNA processing enzyme, RNase P. Yeast mitochondrial RNase P contains an AU-rich mitochondrial coded RNA which varies in size in different yeasts. All of these RNAs contain two short sequences with similarity to two sequences found in all RNase P RNAs.
Kathleen R. Groom   +3 more
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Human RNase P and Transcription

2009
Human nuclear RNase P has been initially characterized by virtue of its ability to process the 5′ leader sequence of precursor tRNA. This ribonucleoprotein complex consists of H1 RNA subunit and at least ten distinct protein components. However, recent findings reveal that RNase P has a role in transcription by RNA polymerase I (Pol I) and Pol III ...
Robert Reiner   +2 more
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Recent Studies of RNase P+

2014
This chapter is primarily a progress report on work with the enzyme from Escherichia coli. RNase P, the endonuclease responsible for the biosynthesis of the 5' termini of mature tRNA, is a ribonucleoprotein. The chapter primarily focuses on relationships between the structure and function of the subunits of RNase P, as determined from studies with the ...
Simon J. Talbot   +2 more
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Characterization of RNase P RNA Activity

2012
The principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts (Trends Genet 19:561-569, 2003; Crit Rev Biochem Mol Biol 41:77-102, 2006; Trends Biochem Sci 31:333-341, 2006).
Markus Gößringer   +2 more
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