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J Olvera

Publications and source records attributed to J Olvera.

At least 37 records · Page 2Linked to original sources

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↗

The primary structure of rat ribosomal protein S5. A ribosomal protein present in the rat genome in a single copy.

The amino acid sequence of the rat 40 S ribosomal subunit protein S5 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed by the determination, directly from the protein, of 17 residues near the NH2 terminus. S5 has 204 amino acids; the molecular weight is 22,863. The protein designated S5a has the same amino acid sequence as S5 except that it lacks the NH2-terminal 5 residues. It is not known whether the conversion of a portion of S5 to S5a is physiological or fortuitous. The mRNA for S5 has about 820 nucleotides. Hybridization of the S5 cDNA to digests of nuclear DNA indicates that the rat genome has only a single copy of the gene; this is in distinction to the mouse and human genomes which have three to six copies of the S5 gene. Rat ribosomal protein S5 is related to the eubacteria, the arachaebacteria, and the chloroplast family of S7 ribosomal proteins. There is a peptide of 16 residues at the carboxyl terminus of S5 that is highly conserved in 18 species spanning the three kingdoms and chloroplasts.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein L11.

The amino acid sequence of the rat 60S ribosomal subunit protein L11 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L11 has 178 amino acids and a molecular weight of 20,239. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 6-8 copies of the L11 gene. The mRNA for the protein is about 800 nucleotides in length. Rat L11 is homologous to ribosomal proteins from other eukaryotes and is related to the L5 family of proteins from eubacterial and archaebacterial ribosomes.

Amino Acid Sequence↗

Primary structure of rat ribosomal protein S2. A ribosomal protein with arginine-glycine tandem repeats and RGGF motifs that are associated with nucleolar localization and binding to ribonucleic acids.

The amino acid sequence of the rat 40 S ribosomal subunit protein S2 was deduced from the sequence of nucleotides in two recombinant cDNAs and confirmed from the amino acid sequence of a cyanogen bromide peptide obtained from the protein. Ribosomal protein S2 has 293 amino acids and has a molecular weight of 31,211. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 23-28 copies of the S2 gene. The mRNA for the protein is about 1,000 nucleotides in length. The highly conserved repetitive mammalian gene family designated LLRep3, but not identified before, encodes ribosomal protein S2. Rat S2 is related to Saccharomyces cerevisiae S4, Methanococcus vannielii S5, Escherichia coli S5, and other members of the prokaryotic S5 family. S. cerevisiae S4 and E. coli S5 are involved in the binding of aminoacyl-tRNA to ribosomes and in conditioning the fidelity of translation; it is plausible to assume that rat S2 serves similar functions. The NH2-terminal region of S2 is rich in arginine-glycine repeats including eight that occur in tandem and has two consecutive copies of the motif RGGF; these sequences have been associated with nucleolar localization and binding to RNA.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S28.

The amino acid sequence of the rat 40S ribosomal subunit protein S28 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein S28 has 69 amino acids and has a molecular weight of 7,836. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 8-10 copies of the S28 gene. The mRNA for S28 is about 450 nucleotides in length. Rat S28 is homologous to Saccharomyces cerevisiae S33.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein L38.

The amino acid sequence of the rat 60S ribosomal protein L38 was deduced from the sequence of nucleotides in three recombinant cDNAs. Ribosomal protein L38 has 69 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 8,081. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 11-13 copies of the L38 gene. The mRNA for the protein is about 450 nucleotides in length.

Amino Acid Sequence↗

Autologous adrenal medullary transplants in advanced Parkinson's disease with particular attention to the selective improvement in symptoms.

Ten patients with advanced Parkinson's disease, presenting with tremor, rigidity and akinesia had autologous adrenal medullary transplantation taken from the left adrenal gland to the head of the right caudate nucleus. Particular attention was taken to avoid prolonged exposure of the adrenal tissue before transplantation and to separate the medullary from the cortical adrenal tissues. Postoperative CT scans confirmed the correct position of the transplants. Differences between pre- and 1-year postoperative clinical conditions were statistically evaluated, with patients under medical (L-dopa) treatment and after the medication was temporarily discontinued. Performance of motor tasks was tested to differentiate slowness of movements imposed by excessive muscular tension (rigidity) from that secondary to delayed reaction time to sensory demands (akinesia). Two deaths occurred 35 and 69 day after surgery for causes not related to the surgical procedures. One of those patients had remained stable neurologically and the other had deteriorated to progressive dementia and catatonia. At autopsy, no lesions in the CNS other than those expected from the surgical procedure were evident, and histological examination failed to reveal chromaffin cells in the head of the right caudate nucleus. Evaluation of the 8 cases that survived for 1 year revealed no significant improvement in their clinical or motor task performance, when considered as a group. However, cases with mild akinesia did better than cases with moderate to advanced akinesia, suggesting that transplantation is indicated in cases with rigidity, but not in cases with 'negative' symptoms of Parkinson's disease. All cases required postoperative medication.

Adrenal Medulla↗

The primary structure of rat ribosomal protein L12.

The covalent structure of the rat 60S subunit protein L12 which is a component of the ribosomal elongation factor binding domain was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. L12 has 165 amino acids and a molecular weight of 17,834. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 11-13 copies of the L12 gene. The mRNA for the protein is about 800 nucleotides in length. Rat L12 is homologous to Saccharomyces cerevisiae L15. The cDNA contains the highly repetitive DNA sequence, R.dre.1, in the 3' noncoding region.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S7.

The amino acid sequence of the rat 40S ribosomal subunit protein S7 was deduced from the sequence of nucleotides in two recombinant cDNAs and confirmed from the amino acid sequence of a cyanogen bromide peptide obtained from the protein. Ribosomal protein S7 has 194 amino acids and has a molecular mass of 22,113. Hybridization of the cDNA to digest of nuclear DNA suggests that there are 14-16 copies of the S7 gene. The mRNA for the protein is about 725 nucleotides in length. Rat S7 is homologous with Xenopus laevis S8. The protein contains a possible internal duplication of 10 residues.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S13.

The covalent structure of the rat 40S ribosomal subunit protein S13 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Rat S13 contains 150 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 17,080. Hybridization of a S13 cDNA to digests of nuclear DNA suggests that there are 8-10 copies of the gene for the protein. The mRNA for the protein is about 620 nucleotides in length. Rat S13 is related to Saccharomyces cerevisiae YS15 and to Halobacterium marismortui S11. The protein contains a possible internal duplication of 12 residues.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein L9.

The amino acid (aa) sequence of rat ribosomal (r) protein L9 was deduced from the nucleotide (nt) sequence in a recombinant cDNA and confirmed from the N-terminal aa sequence of the protein. L9 contains 192 aa and has an Mr of 21879. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 20-23 copies of the L9 gene. The mRNA for the protein is about 800 nt in length. Rat L9 is related to Saccharomyces cerevisiae YL11, Methanococcus vannielii L6, Escherichia coli L6 and other members of the prokaryotic L6 family. The protein contains a possible internal duplication of 11 aa.

Amino Acid Sequence↗

The primary structure of rat ribosomal proteins: the amino acid sequences of L27a and L28 and corrections in the sequences of S4 and S12.

The amino acid sequences of rat ribosomal proteins L27a and L28 were deduced from the sequences of nucleotides in recombinant cDNAs and confirmed from the NH2-terminal amino acid sequences of the proteins. L27a contains 147 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 16 476. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 18-22 copies of the L27a gene. The mRNA for the protein is about 600 nucleotides in length. L27a is homologous to mouse L27a (there are 3 amino acid changes) and to yeast L29. Rat ribosomal protein L28 has 136 amino acids (its NH2-terminal methionine is also processed after translation) and has a molecular weight of 15 707. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 9 or 10 copies of the L28 gene. The mRNA for the protein is about 640 nucleotides in length. L28 contains a possible internal duplication of 9 residues. Corrections are recorded in the sequences reported before for rat ribosomal proteins S4 and S12.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S16.

The amino acid sequence of rat ribosomal protein S16 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. S16 contains 145 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular mass of 16,304. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 11-13 copies of the S16 gene. The mRNA for the protein is about 700 nucleotides in length. Rat S16 is homologous to mouse S16 (there are 2 amino acid changes and a residue is deleted) and related to Halobacterium morismortui ribosomal protein S3 and to Escherichia coli S9.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein L35.

The amino acid sequence of the rat 60S ribosomal subunit protein L35 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 L35 has 122 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 14,412. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 15-17 copies of the L35 gene. The mRNA for the protein is about 570 nucleotides in length. Rat L35 is related to the archaebacterial ribosomal proteins Halobacterium marismortui L33 and Halobacterium halobium L29E; it is also related to Escherichia coli L29 and to other members of the prokaryotic ribosomal protein L29 family. The protein contains a possible internal duplication of 11 residues.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S24.

The amino acid sequence of rat ribosomal protein S24 was deduced from the sequence of nucleotides in a recombinant cDNA. S24 contains 133 amino acids and has a molecular mass of 15,413. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 12-16 copies of the S24 gene. The mRNA for the protein is about 600 nucleotides in length. Rat S24 is homologous to Xenopus laevis S19 and related to Halobacterium morismortui ribosomal protein S15.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S3.

The amino acid sequence of rat ribosomal protein S3, which has been reported to form part of the binding site for initiation factors, was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein S3 contains 243 amino acids and has a molecular weight of 26,643. Rat S3 and Xenopus laevis ribosomal protein S1 are homologous: There are 62 identities in 63 consecutive residues in the carboxyl-terminal amino acid acid sequence of rat S3 and in a partial sequence of Xenopus S1. Hybridization of rat S3 cDNA to digests of nuclear DNA suggests that there are 8-10 copies of the S3 gene. The mRNA for the protein is about 950 nucleotides in length.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein S19.

The covalent structure of rat ribosomal protein S19 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 S19 contains 144 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 15,944. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 15-18 copies of the S19 gene. The mRNA for the protein is about 640 nucleotides in length. Rat S19 is related to Saccharomyces cerevisiae S16A and to Halobacterium marismortui S12.

Amino Acid Sequence↗

The primary structure of rat ribosomal protein L26.

The amino acid sequence of rat ribosomal protein L26 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Rat L26 contains 145 amino acids and has a molecular mass of 17,266 Da. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 8-16 copies of the L26 gene. The mRNA for the protein is about 650 nucleotides in length. Protein L26 has a sequence of 9 residues that may be repeated in three places.

Amino Acid Sequence↗