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Dive into the research topics where Joe Olvera is active.

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Featured researches published by Joe Olvera.


FEBS Letters | 1990

The primary structure of rat ribosomal protein S16.

Yuen-Ling Chan; Veronica Paz; Joe Olvera; Ira G. Wool

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 16304. 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.


Biochimica et Biophysica Acta | 1990

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

Ira G. Wool; Yuen-Ling Chan; Veronica Paz; Joe Olvera

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.


FEBS Letters | 1989

The primary structure of rat ribosomal protein L26

Veronica Paz; Joe Olvera; Yuen-Ling Chan; Ira G. Wool

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.


Biochimie | 1990

The primary structure of rat ribosomal protein S19

Katsuyuki Suzuki; Joe Olvera; Ira G. Wool

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.


Biochemical and Biophysical Research Communications | 1990

The primary structure of rat ribosomal protein S13.

Katsuyuki Suzuki; Joe Olvera; Ira G. Wool

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.


Archives of Biochemistry and Biophysics | 1990

The primary structure of rat ribosomal protein S3

Yuen-Ling Chan; K.R.G. Devi; Joe Olvera; Ira G. Wool

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.


Gene | 1990

The primary structure of rat ribosomal protein L9

Katsuyuki Suzuki; Joe Olvera; Ira G. Wool

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.


Biochemical and Biophysical Research Communications | 1991

The primary structure of rat ribosomal protein L38

Yuh Kuwano; Joe Olvera; Ira G. Wool

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.


FEBS Letters | 1990

The primary structure of rat ribosomal protein S7

Katsuyuki Suzuki; Joe Olvera; Ira G. Wool

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 22113. 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.


Biochemical and Biophysical Research Communications | 1990

The primary structure of rat ribosomal protein L35

Katsuyuki Suzuki; Joe Olvera; Ira G. Wool

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.

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