The requirement for the <i>Escherichia coli</i> ribosomal proteins L7 and L12 in release factor‐dependent peptide chain termination

Armstrong, Ian L.; Tate, Warren P.

doi:10.1016/0014-5793(80)81093-3

FEBS Letters

1980

DOI: 10.1016/0014-5793(80)81093-3

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The requirement for the Escherichia coli ribosomal proteins L7 and L12 in release factor‐dependent peptide chain termination

Ian L. Armstrong¹,

Warren P. Tate²

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1982

2005

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Cited by 12 publications

(3 citation statements)

References 22 publications

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“…A direct and essential involvement of the stalk in the translocation step was soon reported (5) and has recently been confirmed (6)(7)(8). In addition, its implication in the function of initiation (9) and termination factors (10) has been reported as well.…”

mentioning

confidence: 83%

The Acidic Protein Binding Site Is Partially Hidden in the Free Saccharomyces cerevisiae Ribosomal Stalk Protein P0

2005

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The ribosomal stalk is essential for translation; however, its overall structure is poorly understood. Characterization of the region involved in the interactions between protein P0 and the 12 kDa acidic proteins P1 and P2 is fundamental to understand the assembly and function of this structure in the eukaryotic ribosome. The acidic protein content is important for the ribosome efficiency and affects the translation of specific mRNAs. By usage of a series of progressively truncated fragments of protein P0 in the two-hybrid test, a region between positions 213 and 250 was identified as the minimal protein part able to interact with the acidic proteins. Extensions at either end affect the binding capacity of the fragment either positively or negatively depending on the number of added amino acids. Deletions inside the binding region confirm its in vivo relevance since they drastically reduce the P0 interacting capacity with the 12 kDa acidic proteins, which are severely reduced in the ribosome when the truncated protein is expressed in the cell. Moreover, recombinant His-tagged P0 fragments containing the binding site and bound to Ni(2+)-NTA columns can form a complex with the P1 and P2 proteins, which is able to bind elongation factor EF2. The results indicate the existence of a region in P0 that specifically interacts with the acidic proteins. These interactions are, however, hindered by the presence of neighbor protein domains, suggesting the need for conformational changes in the complete P0 to allow the assembly of the ribosomal stalk.

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confidence: 83%

The Acidic Protein Binding Site Is Partially Hidden in the Free Saccharomyces cerevisiae Ribosomal Stalk Protein P0

2005

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“…In Escherichia coli, the acidic L7 and L12 proteins (L7 is the N-acetylated form of L12), present as two dimers in the ribosome (44), are needed for supernatant factordependent reactions (3,4,7,14), and it has been proposed that they are involved in the transduction of energy required for tRNA translocation (14). No functional significance for the presence of the two forms of the bacterial acidic protein L7/L12 has been found, although changes in their ratio have been detected during the cell growth cycle (35).…”

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confidence: 99%

Disruption of single-copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiae.

Remacha¹,

Santos²,

Ballesta³

1990

Mol. Cell. Biol.

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“…The large ribosomal subunit from all organisms contains a set of very acidic proteins which are required for ribosome activity during protein synthesis (see references 6 and 28 for reviews). In Escherichia coli, the acidic L7 and L12 proteins (L7 is the N-acetylated form of L12), present as two dimers in the ribosome (44), are needed for supernatant factordependent reactions (3,4,7,14), and it has been proposed that they are involved in the transduction of energy required for tRNA translocation (14). No functional significance for the presence of the two forms of the bacterial acidic protein L7/L12 has been found, although changes in their ratio have been detected during the cell growth cycle (35).…”

mentioning

confidence: 99%

Disruption of Single-Copy Genes Encoding Acidic Ribosomal Proteins in Saccharomyces cerevisiae

Remacha

Santos

Ballesta

1990

Molecular and Cellular Biology

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Using the cloned genes coding for the ribosomal acidic proteins L44 and L45, constructions were made which deleted part of the coding sequence and inserted a DNA fragment at that site carrying either the URA3 or HIS3 gene. By gene disruption techniques with linearized DNA from these constructions, strains of Saccharomyces cerevisiae were obtained which lacked a functional gene for either protein L44 or protein L45. The disrupted genes in the transformants were characterized by Southern blots. The absence of the proteins was verified by electrofocusing and immunological techniques, but a compensating increase of the other acidic ribosomal proteins was not detected. The mutant lacking L44 grew at a rate identical to the parental strain in complex as well as in minimal medium. The L45-disrupted strain also grew well in both media but at a slower rate than the parental culture. A diploid strain was obtained by crossing both transformants, and by tetrad analysis it was shown that the double transformant lacking both genes is not viable. These results indicated that proteins L44 and L45 are independently dispensable for cell growth and that the ribosome is functional in the absence of either of them.

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The requirement for the Escherichia coli ribosomal proteins L7 and L12 in release factor‐dependent peptide chain termination

Cited by 12 publications

References 22 publications

The Acidic Protein Binding Site Is Partially Hidden in the Free Saccharomyces cerevisiae Ribosomal Stalk Protein P0

The Acidic Protein Binding Site Is Partially Hidden in the Free Saccharomyces cerevisiae Ribosomal Stalk Protein P0

Disruption of single-copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiae.

Disruption of Single-Copy Genes Encoding Acidic Ribosomal Proteins in Saccharomyces cerevisiae

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