Interaction of the release factors with the Escherichia coli ribosome: structurally and functionally-important domains

Asymmetric Interactions between the Acidic P1 and P2 Proteins in the Saccharomyces cerevisiae Ribosomal Stalk

“…A direct confirmation of this association has recently been shown by cryoelectron microscopy (2,3). Involvement of the stalk components has also been reported in initiation (4,5) and termination (6,7).…”

Asymmetric Interactions between the Acidic P1 and P2 Proteins in the Saccharomyces cerevisiae Ribosomal Stalk

“…A direct confirmation of this association has recently been shown by cryoelectron microscopy (2,3). Involvement of the stalk components has also been reported in initiation (4,5) and termination (6,7).…”

Single point mutations in domain II of the yeast mitochondrial release factor mRF-1 affect ribosome binding

“…Moreover, both 530-loop and S4 are implicated in EF-Tu binding and it has been proposed that mutations in these components can cause a ram phenotype by altering the interaction between ribosome and EF-Tu (38). For the present study it is of great interest that E. coli S4 also has been implicated in release factor binding (2,39,40). It has indeed previously been shown that EF-Tu and RF-2 bind E. coli ribosomes in a mutually exclusive manner (41).…”

Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure

“…cross-reacted with B. subtilis RF-2, predicting the presence of a structurally related domain in the latter RF (1). Indeed, the alignment of both RF-2s reveals many positions of identical or related amino acids in this region (Fig.…”

Asymmetric Interactions between the Acidic P1 and P2 Proteins in the Saccharomyces cerevisiae Ribosomal Stalk

“…A direct confirmation of this association has recently been shown by cryoelectron microscopy (2,3). Involvement of the stalk components has also been reported in initiation (4,5) and termination (6,7).…”

Single point mutations in domain II of the yeast mitochondrial release factor mRF-1 affect ribosome binding

“…Moreover, both 530-loop and S4 are implicated in EF-Tu binding and it has been proposed that mutations in these components can cause a ram phenotype by altering the interaction between ribosome and EF-Tu (38). For the present study it is of great interest that E. coli S4 also has been implicated in release factor binding (2,39,40). It has indeed previously been shown that EF-Tu and RF-2 bind E. coli ribosomes in a mutually exclusive manner (41).…”

Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure

“…cross-reacted with B. subtilis RF-2, predicting the presence of a structurally related domain in the latter RF (1). Indeed, the alignment of both RF-2s reveals many positions of identical or related amino acids in this region (Fig.…”

Asymmetric Interactions between the Acidic P1 and P2 Proteins in the Saccharomyces cerevisiae Ribosomal Stalk

“…A direct confirmation of this association has recently been shown by cryoelectron microscopy (2,3). Involvement of the stalk components has also been reported in initiation (4,5) and termination (6,7).…”

Single point mutations in domain II of the yeast mitochondrial release factor mRF-1 affect ribosome binding

“…Moreover, both 530-loop and S4 are implicated in EF-Tu binding and it has been proposed that mutations in these components can cause a ram phenotype by altering the interaction between ribosome and EF-Tu (38). For the present study it is of great interest that E. coli S4 also has been implicated in release factor binding (2,39,40). It has indeed previously been shown that EF-Tu and RF-2 bind E. coli ribosomes in a mutually exclusive manner (41).…”

Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure

“…cross-reacted with B. subtilis RF-2, predicting the presence of a structurally related domain in the latter RF (1). Indeed, the alignment of both RF-2s reveals many positions of identical or related amino acids in this region (Fig.…”