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I G Wool

Publications and source records attributed to I G Wool.

At least 91 records · Page 5Linked to original sources
PubMed1989

The primary structure of rat ribosomal protein S10.

The amino acid sequence of rat ribosomal protein S10 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein S10 contains 165 amino acids and has a molecular mass of 18917 Da. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 17-20 copies of the S10 gene. The mRNA for the protein is about 750 nucleotides in length. Ribosomal protein S10 has several possible internal duplications; one is a tandem repeat of ten residues that is basic and contains two or three prolines.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein L34.

The amino acid sequence of rat ribosomal protein L34 was deduced from the nucleotide sequence in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein L34 contains 117 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has an Mr of 13,498. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 7-9 copies of the L34 gene. The mRNA for the protein is about 630 nucleotides in length.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein L18a.

The amino acid sequence of rat ribosomal protein L18a was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L18a contains 175 amino acids and has a molecular mass of 20,047 Da. Hybridization of the cDNA to digests of rat nuclear DNA and to a preparation of poly(A)+ mRNA suggests that there are 8-11 copies of the L18a gene and that the mRNA for the protein is about 700 nucleotides in length. Rat L18a is related to Schizosaccharomyces pombe L17 and perhaps to Halobacterium marismortui L19.

Amino Acid Sequence↗
PubMed1989

Antiribosomal S10 antibodies in humans and MRL/lpr mice with systemic lupus erythematosus.

Autoantibodies directed against a ribosomal small subunit protein of 20,000 molecular weight were found in sera from 5 of 44 patients with systemic lupus erythematosus (11%) and 5 of 48 MRL/lpr mice (10%). This ribosomal protein was identified as S10 on the basis of two-dimensional gel electrophoresis and immunoblotting, as well as immunoblots of the purified S10 protein. The S10 protein antigen was readily extracted from ribosomes at low salt (300 mM KCl) and low magnesium (0.5 mM) concentrations, consistent with the highly exposed location proposed for this protein on the 40S subunit. Anti-S10 antibodies were observed significantly more frequently in lupus sera containing both anti-Sm and antiribosomal P protein antibodies and in MRL/lpr sera with anti-Sm activity, suggesting a linked pattern of autoantibody response. Together with anti-Sm and antiribosomal P protein antibodies, anti-S10 represents a third autoantibody highly specific for lupus in humans and MLR/lpr mice.

Animals↗
PubMed1988

The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid.

An oligoribonucleotide (35-mer) that mimics the alpha-sarcin and the ricin region of eukaryotic 28 S rRNA was transcribed in vitro from a synthetic template with T7 RNA polymerase and was used to test whether the specificity of the hydrolysis by the toxins was retained. alpha-Sarcin, at a low concentration, cleaved a single phosphodiester bond on the 3' side of a guanosine residue in the synthetic oligomer that corresponds to G-4325 in 28 S rRNA, the site of action of the toxin in intact ribosomes. At a high concentration of alpha-sarcin, the substrate (35-mer) was hydrolyzed after each of its purines. alpha-Sarcin was without an effect on a synthetic RNA (20-mer) that reproduces the near universal sequence of nucleotides in the loop, but lacks the stem, of the toxin's domain. Thus, the specificity of the attack of alpha-sarcin on a precise region of 28 S rRNA appears to be contingent on the sequence of the nucleotides and the structure of the domain. Ricin depurinated a nucleotide in the synthetic oligomer (35-mer), and in the presence of aniline the phosphoribose backbone was cleaved at a position that conforms to A-4324 in 28 S rRNA, the site of action of the toxin in vivo.

Base Sequence↗
PubMed1988

The primary structure of rat ribosomal protein S6.

The amino acid sequence of rat ribosomal protein S6, the major phosphoprotein in the organelle, was deduced from the sequence of nucleotides in two recombinant cDNAs and confirmed from the sequence of amino acids in portions of the protein. Ribosomal protein S6 contains 249 amino acids and has a molecular weight of 28,683. The protein has 15 seryl residues; 7 are located in the carboxyl-terminal sequence of 15 amino acids and probably include most if not all of the residues that are phosphorylated. There are related repeated sequences of 10 amino acids each that occur at four separate positions in S6 and that are very basic. Rat S6 is homologous to Saccharomyces cerevisiae S10 (the extent of the identity is 75%) and most likely also to Schizosaccharomyces pombe S6.

Amino Acid Sequence↗
PubMed1988

The primary structure of rat ribosomal protein L18.

The amino acid sequence of rat ribosomal protein L18 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the amino-terminal amino acid sequence of the protein. Ribosomal protein L18 contains 187 amino acids (the amino-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 21,530. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 10-14 copies of the L18 gene. Rat ribosomal protein L18 is homologous to Xenopus laevis L14; the extent of the identity of the amino acid sequences is 87% and for the nucleotides in the coding region of the DNA it is 76%.

Amino Acid Sequence↗
PubMed1988

Primary structure of rat ribosomal protein L36a.

The amino acid sequence of rat ribosomal protein L36a, which may form part of the peptidyl transferase center, was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the amino-terminal amino acid sequence of the protein. Ribosomal protein L36a contains 105 amino acids (the amino-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 12,311. Hybridization of the cDNA to digests of nuclear DNA suggests that there are multiple copies of the L36a gene. Rat ribosomal protein L36a is homologous to a protein HL44 present in ribosomes of humans and protein 44 from Saccharomyces cerevisiae ribosomes.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein S8.

The amino acid sequence of rat ribosomal protein S8 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2- and carboxyl-terminal amino acid sequences of the protein. Ribosomal protein S8 contains 207 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 23,928. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 7-9 copies of the S8 gene. Ribosomal protein S8 contains a possible internal repeat that has 12 or 13 residues, is basic, and occurs 5 times in the protein.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein S12. The relationship of rat S12 to other ribosomal proteins and a correlation of the amino acid sequences of rat and yeast ribosomal proteins.

The covalent structure of the rat 40 S ribosomal subunit protein S12 was determined from the sequence of amino acids in tryptic, chymotryptic, thermolytic, and cyanogen bromide peptides and inferred from the sequence of nucleotides in a recombinant cDNA. Rat ribosomal protein S12 contains 129 amino acids and has a molecular weight of 14,120. The amino acid sequences of a number of ribosomal proteins appear to be related to rat S12. These include spinach chloroplast L7, Escherichia coli S5, Nicotiana tabacum chloroplast S18, and Bacillus stearothermophilus S12, and perhaps others. In addition, there are two sequences, 26 and 18 amino acids in length, in rat S12 that may be related to segments of the same number of residues in ribosomal proteins from a number of species. These, and other results, reinforce the suggestion that ribosomal proteins form an extended family.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein L7. The presence near the amino terminus of L7 of five tandem repeats of a sequence of 12 amino acids.

The covalent structure of rat ribosomal protein L7 was determined in part from the sequence of nucleotides in a recombinant cDNA and in part from the sequence of amino acids in portions of the protein. The complementary analyses supplemented and confirmed each other. Ribosomal protein L7 contains 258 amino acids and has a molecular weight of 30,040. The protein has an unusual and striking structural feature near the NH2 terminus: five tandem repeats of a sequence of 12 residues. Rat L7 appears to be related to ribosomal protein L7 from the moderate halophile Vibrio costicola and perhaps to L30 from Bacillus stearothermophilus, to L7 from the moderate halophile NRCC 41227, and to L22 from Nicotinia tobaccum chloroplast. In addition, there is a sequence of 24 amino acids in rat protein L7 that may be related to segments of the same number of residues in Escherichia coli ribosomal proteins S10, S15, L9, and L22.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA.

The covalent structure of rat ribosomal protein L5, which associates with 5 S rRNA in the organelle, was deduced from the sequence of nucleotides in a recombinant cDNA (pL5-6-4) and confirmed from the sequences of amino acids in portions of the protein. Ribosomal protein L5, encoded by pL5-6-4, contains 296 amino acids and has a molecular weight of 34,298. However, a second recombinant cDNA, pL5-8-5, encodes a protein with an additional methionyl residue at position 236 and may be the product of a second active L5 gene. Rat L5 is homologous to yeast YL3 and to Halobacterium cutirubrum HL13, proteins that also bind to 5 S rRNA. No significant structural similarity, however, was found between rat L5 and other 5 S rRNA-binding proteins; not with a second H. cutirubrum protein HL19, nor the Escherichia coli ribosomal proteins, L5, L18, or L25, nor the Xenopus laevis transcription factor IIIA. H. cutirubrum HL19, however, has structural identity with E. coli L5 and seems to be related to yeast YL3 and, hence, may be an evolutionary link between the prokaryotic and eukaryotic 5 S rRNA-binding proteins. A group of ribosomal proteins not known to be associated with 5 S rRNA are also related to rat L5. They include: rat L39, Euglina gracilis chloroplast S7, Saccharomyces cerevisiae L31 and L46, Homo sapiens L32 and, perhaps, several others as well. There is an especially close interrelationship between rat L5, rat L39, yeast L46, human L32, and mouse L32. These results, and others, suggest that ribosomal proteins form an extended family and that L5 may contain in its structure traces of this affinity.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein L19. A determination from the sequence of nucleotides in a cDNA and from the sequence of amino acids in the protein.

The covalent structure of rat ribosomal protein L19 was inferred from the sequence of nucleotides in a recombinant cDNA and confirmed from the sequence of amino acids in a portion of the protein. Ribosomal protein L19 contains 196 amino acids and has a molecular weight of 26,971. There are indications that a segment of 23 residues in rat L19 is related to sequences of the same length in Escherichia coli ribosomal proteins L30, L18, and S2.

Amino Acid Sequence↗
PubMed1986

Use of the cytotoxic nuclease alpha-sarcin to identify the binding site on eukaryotic 5 S ribosomal ribonucleic acid for the ribosomal protein L5.

Treatment of the large subunit of eukaryotic ribosomes with EDTA releases a 7 S ribonucleoprotein complex that contains protein L5 and 5 S rRNA. The region of rat 5 S rRNA that is protected by protein L5 from digestion with the ribonuclease alpha-sarcin includes nucleotides 1-10, 12-22, and 64-116. This domain approximates the combined binding sites for the three proteins (L5, L18, and L25) that associate with Escherichia coli 5 S rRNA. In addition, the region of 5 S rRNA protected by rat ribosomal protein L5 corresponds closely to that occupied by Xenopus transcription factor IIIA.

Animals↗
PubMed1986

Identification of the binding site on 5S rRNA for the transcription factor IIIA: proposed structure of a common binding site on 5S rRNA and on the gene.

Transcription factor IIIA interacts specifically with an internal control region of Xenopus 5S ribosomal RNA genes and is also a component, along with 5S rRNA, of a 7S ribonucleoprotein particle present in previtellogenic oocytes. We have determined the region of the 5S rRNA in the 7S ribonucleoprotein complex that is protected by the transcription factor from digestion with the ribonuclease alpha-sarcin. The binding site for factor IIIA extends from nucleotide 64 through nucleotide 116; the protected region includes two CCUGG helices separated by 11 nucleotides. The same helices occur in the factor IIIA binding site in the 5S rRNA gene and may constitute a common structural feature recognized by the protein in the gene and in the gene product.

Animals↗