It was recently demonstrated that peptide bond formation can occur using an Escherichia coli naked 23S ribosomal RNA without any of the ribosomal pro-teins. Here, the six domains of the 23S ribosomal RNA were individually synthesized and shown to be capable, when complexed together, of stimulating the reaction. Omission and addition experiments indicated that the activity could be reconstituted solely by domain V at a concentration 10 times higher than that of the intact 23S ribosomal RNA, whereas domain VI could enhance the activity in trans. These Þndings suggest that fragments of an RNA molecule have the ability to associate into a functional whole. The complete sequence of E. coli 23S ribo-somal RNA (rRNA) was first determined in 1980; ...
AbstractBackground: One of the most significant questions in understanding the origin of life concer...
Ribosome, the ubiquitous organelle, is the site for protein synthesis in all types of cells. The con...
High-resolution crystal structures of large ribosomal subunits from Deinococcus radiodurans complexe...
It was recently demonstrated that peptide bond formation can occur using an Escherichia coli naked 2...
Peptides of defined length carrying a diazirine photo-affinity label attached either to the a-NH2 gr...
A stable homogeneous ribonucleoprotein fragment of the 30 S ribosomal subunit of E_. coli has been p...
Many methods have been used for investigating the structural organisation of the ribosome. Although ...
Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichi...
In this issue of Chemistry & Biology, Lang et al. (2008) add an important step toward a molecular un...
Abstract. Investigations that are being carried out in various laboratories including ours clearly p...
AbstractHelix 89 of the 23S rRNA connects ribosomal peptidyltransferase center and elongation factor...
Ribosomes, the universal cellular organelles catalyzing the translation of genetic code into protein...
SummaryPeptide bond formation is a fundamental reaction in biology, catalyzed by the ribosomal pepti...
The RNA binding capacity of 50S proteins from E. coli ribo-somes has been tested under improved cond...
The complexity of translation is a classical dilemma in the evolution of biological systems. Efficie...
AbstractBackground: One of the most significant questions in understanding the origin of life concer...
Ribosome, the ubiquitous organelle, is the site for protein synthesis in all types of cells. The con...
High-resolution crystal structures of large ribosomal subunits from Deinococcus radiodurans complexe...
It was recently demonstrated that peptide bond formation can occur using an Escherichia coli naked 2...
Peptides of defined length carrying a diazirine photo-affinity label attached either to the a-NH2 gr...
A stable homogeneous ribonucleoprotein fragment of the 30 S ribosomal subunit of E_. coli has been p...
Many methods have been used for investigating the structural organisation of the ribosome. Although ...
Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichi...
In this issue of Chemistry & Biology, Lang et al. (2008) add an important step toward a molecular un...
Abstract. Investigations that are being carried out in various laboratories including ours clearly p...
AbstractHelix 89 of the 23S rRNA connects ribosomal peptidyltransferase center and elongation factor...
Ribosomes, the universal cellular organelles catalyzing the translation of genetic code into protein...
SummaryPeptide bond formation is a fundamental reaction in biology, catalyzed by the ribosomal pepti...
The RNA binding capacity of 50S proteins from E. coli ribo-somes has been tested under improved cond...
The complexity of translation is a classical dilemma in the evolution of biological systems. Efficie...
AbstractBackground: One of the most significant questions in understanding the origin of life concer...
Ribosome, the ubiquitous organelle, is the site for protein synthesis in all types of cells. The con...
High-resolution crystal structures of large ribosomal subunits from Deinococcus radiodurans complexe...