The primary structure of protein L17 from the <i>Escherichia coli</i> ribosome

Rombauts, Wilfried; Feytons, Valère; Wittmann‐Liebold, Brigitte

doi:10.1016/0014-5793(82)81124-1

Cited by 12 publications

(5 citation statements)

References 21 publications

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“…In addition, it confirms and refines the published amino acid sequences for the five proteins encoded by the operon. The DNA sequence of the S13, Sll, alpha and L17 genes show complete agreement with the published amino acid sequences of the protein products of these qenes (31)(32)(33)(34).…”

Section: Ctgggcatgcgcctggaaaactggccaccggcaagcatcgctgacgagtaaccggatcacsupporting

confidence: 78%

Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli

et al. 1985

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In Escherichia coli some 19 transcription units encoding the 52 ribosomal proteins are scattered throughout the genome. One of the units, the alpha operon, encodes genes for the ribosomal proteins S13, S11, S4 and L17 as well as the alpha subunit of RNA polymerase. We report here the complete 3.0 kb nucleotide sequence of the alpha operon. In addition, we have determined by S1 nuclease mapping the site of transcription termination in this operon.

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Section: Ctgggcatgcgcctggaaaactggccaccggcaagcatcgctgacgagtaaccggatcacsupporting

confidence: 78%

Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli

et al. 1985

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“…The amino acid sequence of the protein encoded by the gene was then compared with E. coli and yeast cytoplasmic ribosomal proteins. The computer search revealed that two stretches in the N-terminal half of this protein had a high degree of similarity to the E. coli r-protein L17 (EL17) (39), although this protein is much smaller than protein YmL8. As shown in Fig.…”

Section: Bpmentioning

confidence: 99%

“…Similarity between the protein encoded by the MRP-L8 gene and ribosomal proteins EL17(39) and ES13 (41) from E. coli and BL17(40) from B. stearothermophilus. The amino acid residues identical with YmL8 are boxed and similar amino acid residues are marked with colons.…”

mentioning

confidence: 99%

Cloning and characterization of nuclear genes for two mitochondrial ribosomal proteins inSaccharomyces cerevisiae

Kitakawa

Grohmann

Graack³

et al. 1990

Nucl Acids Res

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The genes for two large subunit proteins, YmL8 and YmL20, of the mitochondrial ribosome of Saccharomyces cerevisiae were cloned by hybridization with synthetic oligonucleotide mixtures corresponding to their N-terminal amino acid sequences. They were termed MRP-L8 and MRP-L20, respectively, and their nucleotide sequences were determined using a DNA sequencer. The MRP-L8 gene was found to encode a 26.8-kDa protein whose deduced amino acid sequence has a high degree of similarity to ribosomal protein L17 of Escherichia coli. The gene MRP-L20 was found to encode a 22.3-kDa protein with a presequence consisting of 18 amino acid residues. By Southern blot hybridization to the yeast chromosomes separated by field-inversion gel electrophoresis, the MRP-L8 and MRP-L20 genes were located on chromosomes X and XI, respectively. Gene disruption experiments indicate that their products, YmL8 and YmL20 proteins, are essential for the mitochondrial function and the absence of these proteins causes instability of the mitochondrial DNA.

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“…To go further in the characterization of the reactive arginine residue a partial hydrolysis was carried out on the Ca# + -ATPase prelabelled with ["%C]PGO. A mild acid hydrolysis can be achieved by incubating with 0.06 M HCl for 16 h. Under these conditions preferentially peptidic bonds at aspartic acid residues become hydrolysed [43]. After purification of the radioactive peptides only two majors bands were visible by SDS\PAGE with molecular masses of 10 600 Da (band I) and 4000 Da (band II).…”

Section: Localization Of Pgo Reactive Sites In the Ca 2 + -Atpasementioning

confidence: 99%

Involvement of an arginyl residue in the nucleotide-binding site of Ca2+-ATPase from sarcoplasmic reticulum as seen by reaction with phenylglyoxal

Corbalán-Garcı́a

Teruel

Gómez‐Fernández

1996

Biochemical Journal

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1. Chemical modification of the Ca(2+)-ATPase with phenylglyoxal, as a modifier of arginine residues, leads to an almost total loss of the ATPase activity. The presence of nucleotides in the reaction medium protects against the binding of 18 nmol of phenylglyoxal/mg of protein and this reduction in the binding of phenylglyoxal is accompanied by a substantial retention of ATPase activity. The incorporation of phenylglyoxal to the protein alters neither calcium binding nor phosphorylation from inorganic phosphate. Nevertheless the binding of nucleotides is dramatically inhibited and, consequently, so is phosphorylation from ATP. Fluorescein 5'-isothiocyanate labelling of the phenylglyoxal-modified ATPase is not affected but, on the other hand, phenylglyoxal is not able to modify the fluorescein 5'-isothiocyanate-prelabelled ATPase. The way in which ATPase inhibition depends on the presence of phenylglyoxal indicates that this process occurs in a pseudo-first-order reaction. However, the dependence of the apparent first-order rate constant on phenylglyoxal concentration appears to be more complex and an inhibition mechanism of two steps, with phenylglyoxal binding, has to be taken into account. 2. We have found that phenylglyoxal labels both A and B tryptic fragments, but only B fragment labelling is prevented by ATP. The sequencing of peptides from mild acid hydrolysis of phenylglyoxal-labelled ATPase shows that phenylglyoxal is located in the Ala506-Gly595 peptide that is a part of the B fragment. 3. We conclude that phenylglyoxal inactivates the calcium pump in a two-step mechanism in which the second step is irreversible. Phenylglyoxal labels an arginyl residue in the Ala506-Gly595 peptide that can be protected by the binding of ATP to its site.

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The primary structure of protein L17 from the Escherichia coli ribosome

Cited by 12 publications

References 21 publications

Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli

Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli

Cloning and characterization of nuclear genes for two mitochondrial ribosomal proteins inSaccharomyces cerevisiae

Involvement of an arginyl residue in the nucleotide-binding site of Ca2+-ATPase from sarcoplasmic reticulum as seen by reaction with phenylglyoxal

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