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Structure and Function of Archaeal Ribonuclease P
2017Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA) and other small RNAs in all phylogenetic domains. A characteristic feature of archaeal RNase P RNAs is that they alone have, unlike bacterial counterparts, little pre-tRNA cleavage activity, but the interaction with ...
Takashi Nakashima +5 more
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Journal of Molecular Biology, 1981
A strain of Escherichia coli lacking RNAase III and containing thermolabile RNAase E and RNAase P was labeled with 32Pi at a non-permissive temperature. RNA molecules were separated by two-dimensional polyacrylamide gel electrophoresis. Most of the small RNA species were isolated and analyzed for the presence of 5′ nucleoside triphosphates.
David Apirion, Greg Plautz
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A strain of Escherichia coli lacking RNAase III and containing thermolabile RNAase E and RNAase P was labeled with 32Pi at a non-permissive temperature. RNA molecules were separated by two-dimensional polyacrylamide gel electrophoresis. Most of the small RNA species were isolated and analyzed for the presence of 5′ nucleoside triphosphates.
David Apirion, Greg Plautz
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Ribonucleoprotein Ribonucleases P and MRP
2011Ribonucleoprotein 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.
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Structural Studies of Ribonuclease P
2009RNase P is a universal ribozyme involved in RNA processing, in particular the maturation of the 5′ end of tRNA. Unlike most naturally occurring ribozymes, it recognizes and cleaves its substrate in trans and is capable of multiple turnovers. RNase P is a ribonucleoprotein complex containing one RNA subunit and as few as one protein subunit.
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