Biomedical subjects

I G Wool

Publications and source records attributed to I G Wool.

At least 37 records · Page 2Linked to original sources

PubMed1995

The primary structures of rat ribosomal proteins: the characterization of the cDNAs for S21 and L39, corrections in the sequences of L7 and L18a, and the identification of L33.

cDNAs for rat ribosomal proteins S21 and L39 were characterized. S21 has 83 amino acids and a molecular weight of 9,121; L39 has 50 amino acids and a molecular weight of 6,271. There are 8 to 9 copies of the S21, and 9 to 11 copies of the L39 genes. The mRNA for S21 is about 500 nucleotides in length and for L39 it is about 450. Rat S21 and L39 are related to ribosomal proteins from other species. Corrections have been made in the amino acid sequences of L7 and L18a. The rat ribosomal protein designated L33 from its coordinates on two-dimensional gels has been found, from its amino acid sequence, to be identical to S24.

Amino Acid Sequence↗

PubMed1995

The primary structure of rat ribosomal protein L22.

The amino acid sequence of the rat 60S ribosomal subunit protein L22 was deduced from the sequence of nucleotides in two recombinant cDNAs. Ribosomal protein L22 has 128 amino acids; the molecular weight is 14,779. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 6 to 9 copies of the L22 gene. The mRNA for the protein is about 600 nucleotides in length. Rat L22 is related to ribosomal proteins from other eukaryotes and is identical in amino acid sequence to human EAP, the EBER 1 (Epstein-Barr virus encoded RNA) associated protein.

Amino Acid Sequence↗

PubMed1994

Analysis of the contribution of an amphiphilic alpha-helix to the structure and to the function of ricin A chain.

The A chain of ricin is a cytotoxic RNA N-glycosidase that inactivates eukaryotic ribosomes. The contribution of the amphiphilic helix D, which is distant from the active site, to the catalysis of the depurination of the adenosine at position 4324 in 28S rRNA has been examined by systematic deletion of amino acids. Two sets of consecutive two- or three-amino acid deletions of the 12 residues in helix D, a total of 20 mutants, were constructed. All 12 of the amino acids could be deleted in one mutant or another without loss of activity; however, mutations that disrupted the amphiphilicity of the helix led to inactivation of the enzyme. Thus, the minimum contribution of helix D to the structure of the ricin A chain is to provide hydrophobic and hydrophilic surfaces to shield helix E, which has the active-site residues; moreover, no amino acid side chain in helix D makes a specific contribution to the recognition of the RNA substrate or to catalysis; and, finally, phasing of the amino acid deletions can be important to the phenotype of mutants.

Amino Acid Sequence↗

PubMed1994

The primary structure of rat ribosomal protein L24.

The amino acid sequence of the rat 60S ribosomal subunit protein L24 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L24 has 157 amino acids; the molecular weight is 17,767. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 9 to 11 copies of the L24 gene. The mRNA for the protein is about 650 nucleotides in length. Rat L24 is related to ribosomal proteins from other eukaryotes and from archaebacteria.

Amino Acid Sequence↗

PubMed1994

The primary structure of rat ribosomal protein S23.

The amino acid sequence of the rat 40S ribosomal subunit protein S23 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein S23 has 142 amino acids, the NH2-terminal methionine is removed after translation of the mRNA, and a molecular weight of 15,666. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 6 to 13 copies of the S23 gene. The mRNA for the protein is about 650 nucleotides in length. Rat S23 is identical to a human ribosomal protein and is also related to Saccharomyces cerevisiae S28, to Tetrahymena thermophila S12, and to the prokaryotic S12 family of ribosomal proteins.

Amino Acid Sequence↗

PubMed1994

The primary structure of rat ribosomal protein L13.

The amino acid sequence of the rat 60S ribosomal subunit protein L13 was deduced from the sequence of nucleotides in two recombinant cDNAs. Ribosomal protein L13 has 210 amino acids, the NH2-terminal methionine is removed after translation of the mRNA and has a molecular weight of 24,094. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 8 to 10 copies of the L13 gene. The mRNA for the protein is about 870 nucleotides in length. Rat L13 is related to ribosomal proteins from other eukaryotes.

Amino Acid Sequence↗

PubMed1994

The primary structure of rat ribosomal protein L15.

The amino acid sequence of the rat 60S ribosomal subunit protein L15 was deduced from the sequence of nucleotides in two recombinant cDNAs. Ribosomal protein L15 has 203 amino acids, the NH2-terminal methionine is removed after translation of the mRNA, and has a molecular weight of 24,000. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 13 to 15 copies of the L15 gene. The mRNA for the protein is about 850 nucleotides in length. Rat L15 is related to ribosomal proteins from other eukaryotes. Rat L15 has the hexapeptide, TYKFFE, that also occurs in the amyloidogenic glycoprotein A4 which is associated with Alzheimer's disease and Down's Syndrome.

Amino Acid Sequence↗

PubMed1994

The primary structure of rat ribosomal protein S15a.

The amino acid sequence of the rat 40S ribosomal subunit protein S15a was deduced from the sequence of nucleotides in two recombinant cDNAs. Ribosomal protein S15a has 129 amino acids, the NH2-terminal methionine is removed after translation of the mRNA and has a molecular weight of 14,698. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 10 to 15 copies of the S15a gene. The mRNA for the protein is about 650 nucleotides in length. Rat S15a is related to ribosomal proteins from other eukaryotes, from eubacteria, and from archaebacteria.

Amino Acid Sequence↗

PubMed1994

A leucine zipper-like motif and a basic region-leucine zipper-like element in rat ribosomal protein L13a. Identification of the tum- transplantation antigen P198.

The amino acid sequence of the rat 60 S ribosomal subunit protein L13a was deduced from the sequence of nucleotides in two recombinant cDNAs. Mature ribosomal protein L13a has 202 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and a M(r) of 23,330. Hybridization of the L13a cDNA to digests of nuclear DNA suggests that there are 9-11 copies of the L13a gene. The mRNA for the protein is approximately 800 nucleotides in length. Rat L13a is related to the Saccharomyces cerevisiae ribosomal proteins that have been provisionally designated rp22 and rp23 and to the eubacterial and archaebacterial family of L13 ribosomal proteins. The mouse tum- transplantation antigen P198 is a mutant of the mouse homolog of rat ribosomal protein L13a. Rat ribosomal protein L7 has, at its NH2 terminus, five tandem repeats of a similar sequence of 12 amino acids (Lin, A., Chan, Y. L., McNally, J., Peleg, D., Meyuhas, O., and Wool, I. G. (1987) J. Biol. Chem. 262, 12665-12671); L13a has, in its carboxyl-terminal region, amino acid sequences with significant identity to L7 repeats 1, 3, and 5. L13a also has a number of short amino acid sequences that are repeated, a leucine zipper-like motif at its NH2 terminus, and a potential basic region-leucine zipper element in its carboxyl-terminal region.

Amino Acid Sequence↗

PubMed1994

The ribosomal RNA identity elements for ricin and for alpha-sarcin: mutations in the putative CG pair that closes a GAGA tetraloop.

alpha-Sarcin is a ribonuclease that cleaves the phosphodiester bond on the 3' side of G4325 in 28S rRNA; ricin A-chain is a RNA N-glycosidase that depurinates the 5' adjacent A4324. These single covalent modifications inactivate the ribosome. An oligoribonucleotide that reproduces the structure of the sarcin/ricin domain in 28S rRNA was synthesized and mutations were constructed in the 5' C and the 3' G that surround a GAGA tetrad that has the sites of toxin action. Covalent modification of the RNA by ricin, but not by alpha-sarcin, requires a Watson-Crick pair to shut off a putative GAGA tetraloop. Either the recognition elements for the two toxins are different despite their catalyzing covalent modification of adjacent nucleotides in 28S rRNA or there are transitions in the conformation of the alpha-sarcin/ricin domain in 28S rRNA and one conformer is recognized by alpha-sarcin and the other by ricin A-chain.

Base Sequence↗

PubMed1993

The conformation of the sarcin/ricin loop from 28S ribosomal RNA.

The sarcin/ricin loop is a highly conserved sequence found in the RNA of all large ribosomal subunits. The cytotoxins alpha-sarcin and ricin both inactivate ribosomes by cleaving a single bond in that loop. Once it has been attacked, ribosomes no longer interact with elongation factors properly, and translation stops. We have determined the conformation of the sarcin/ricin loop by multinuclear NMR spectroscopy using E73, a 29-nucleotide RNA that has the sarcin/ricin loop sequence and that is sensitive to both toxins in vitro. The sarcin/ricin loop has a compact structure that contains several purine.purine base pairs, a GAGA tetraloop, and a bulged guanosine adjacent to a reverse Hoogsteen A.U pair. It is stabilized by an unusual set of cross-strand base-stacking interactions and imino proton to phosphate oxygen hydrogen bonds. In addition to having interesting structural features, this model explains many of the biochemical observations made about the loop's structure and its reactivity with cytotoxins, and it sheds light on the loop's interactions with elongation factors.

Animals↗

PubMed1993

The carboxyl extension of a ubiquitin-like protein is rat ribosomal protein S30.

The amino acid sequence of the rat 40 S ribosomal subunit protein S30 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed by the determination of the 18 residues at the NH2 terminus of the protein. Unlike the majority of ribosomal proteins, which are unprocessed primary products of the translation of their mRNAs, S30 is formed by cleavage from a larger hybrid protein. The NH2-terminal polypeptide has 38% identity with ubiquitin and contains the characteristic carboxyl-terminal Gly-Gly dipeptide of this family of proteins. S30 has 59 amino acids and the molecular weight is 6,643; the ubiquitin-like sequence has 74 residues and the molecular weight is 7,634. The hybrid protein is encoded in each of the 8-10 members of the family of rat S30 genes; there is, however, only a single species of mRNA which contains the sequences for both proteins. The coding sequence of the hybrid protein occurs in the reverse polarity in the genome of the Finkel-Biskis-Reilly murine sarcoma virus.

Amino Acid Sequence↗

PubMed1993

The primary structure of rat ribosomal protein S9.

The amino acid sequence of the rat 40S ribosomal subunit protein S9 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein S9 has 193 amino acids, the NH2-terminal methionine is removed after translation of the mRNA, and has a molecular weight of 22,360. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 14 to 16 copies of the S9 gene. The mRNA for the protein is about 1,000 nucleotides in length in part because of an especially long 5' noncoding region (103 nucleotides). Rat S9 is related to ribosomal proteins from other eukaryotes, Saccharomyces cerevisiae YS11 and Dictyostelium discoideum rp 1024, and to the eubacterial, archaebacterial, and chloroplast family of S4 ribosomal proteins. We have identified the product of the Trypanosoma brucei gene U as the homolog of rat ribosomal protein S9.

Amino Acid Sequence↗

PubMed1993

The primary structure of rat ribosomal protein L29.

The amino acid sequence of the rat 60S ribosomal subunit protein L29 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L29 has 155 amino acids, the NH2-terminal methionine is removed after translation of the mRNA, and has a molecular weight of 17,183. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 20 to 22 copies of the L29 gene. The mRNA for the protein is about 750 nucleotides in length. Rat L29 is related to yeast ribosomal protein YL43.

Amino Acid Sequence↗

PubMed1993

The primary structure of L37--a rat ribosomal protein with a zinc finger-like motif.

The amino acid sequence of the rat 60S ribosomal subunit protein L37 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L37 has 96 amino acids, the NH2-terminal methionine is removed after translation of the mRNA, and has a molecular weight of 10,939. Ribosomal protein L37 has a single zinc finger-like motif of the C2-C2 type. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 13 or 14 copies of the L37 gene. The mRNA for the protein is about 500 nucleotides in length. Rat L37 is related to Saccharomyces cerevisiae ribosomal protein YL35 and to Caenorhabditis elegans L37. We have identified in the data base a DNA sequence that encodes the chicken homolog of rat L37.

Amino Acid Sequence↗

PubMed1993

The primary structure of rat ribosomal protein L36.

The amino acid sequence of the rat 60S ribosomal subunit protein L36 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L36 has 104 amino acids, the NH2-terminal methionine is removed after translation of the mRNA and has a molecular weight of 12,128. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 8 to 11 copies of the L36 gene. The mRNA for the protein is about 500 nucleotides in length. Rat L36 is related to yeast ribosomal protein YL39.

Amino Acid Sequence↗

PubMed1993

Zinc finger-like motifs in rat ribosomal proteins S27 and S29.

The primary structures of the rat 40S ribosomal subunit proteins S27 and S29 were deduced from the sequences of nucleotides in recombinant cDNAs and confirmed by determination of amino acid sequences in the proteins. Ribosomal protein S27 has 83 amino acids and the molecular weight is 9,339. Hybridization of cDNA to digests of nuclear DNA suggests that there are 4-6 copies of the S27 gene; the mRNA for the protein is about 620 nucleotides in length. Ribosomal protein S29 has 55 amino acids and the molecular weight is 6,541. There are 14-17 copies of the S29 gene and its mRNA is about 500 nucleotides in length. Rat ribosomal protein S29 is related to several members of the archaebacterial and eubacterial S14 family of ribosomal proteins. S27 and S29 have zinc finger-like motifs as do other proteins from eukaryotic, archaebacterial, eubacterial, and mitochondrial ribosomes. Moreover, ribosomes and ribosomal subunits appear to contain zinc and iron as well.

Amino Acid Sequence↗

PubMed1993

The primary structure of rat ribosomal protein L23a. The application of homology search to the identification of genes for mammalian and yeast ribosomal proteins and a correlation of rat and yeast ribosomal proteins.

The amino acid sequence of the rat 60 S ribosomal subunit protein L23a was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L23a has 156 amino acids and a molecular weight of 17,684. Hybridization of the L23a cDNA to digests of nuclear DNA suggests that there are 18-20 copies of the L23a gene. The mRNA for the protein is about 600 nucleotides in length. Rat L23a is related to the yeast Saccharomyces cerevisiae L25, to the archaebacterial Methanococcus vannielii L23, to eubacterial Escherichia coli L23, and to other members of the L23 family of ribosomal proteins. A novel application of a routine homology search procedure was employed to identify a nucleotide sequence that could be used to design an oligodeoxynucleotide probe to screen a library for a cDNA that encodes rat L23a; this same procedure uncovered a number of previously unidentified genes for yeast ribosomal proteins in the GenBank DNA data base. In a correlation of rat and yeast ribosomal proteins 48 pairs are shown to be related.

Amino Acid Sequence↗