The nucleotide sequence of 5S rRNA from bovine liver.

We have determined the nucleotide sequence of ribosomal 5S RNA from bovine liver. The comparison of this sequence with those from other eukaryotic sources shows that a common secondary structure model for all eukaryotic 5S rRNAs may exist. Analysis of the evolutionary conserved nucleotides in metazoan 5S rRNAs suggests that the tertiary interactions, proposed earlier for plant 5S rRNA, are also possible.     

The nucleotide sequence of tyrosine tRNAQ* psi A from bovine liver

The nucleotide sequence of tyrosine tRNAQ* psi A from bovine liver was determined to be pC-C-U-U-C-m2G-A-U-A-m2G-C-U-C-A-G-D-D-G-G-acp3U-A-G-A -G-C-m22G-m22G -A-G-G-A-C-U-Q*-psi-A-m1G-A-psi m-C-C-U-U-A-G-m7G-D-m5C-G-C-U-G-G-T-psi-C-G-m1A -U-U-C-C-G-G-C-U-C-G-A-A-G-G-A-C-C-AOH. This tyrosine tRNA is 76 nucleotides in length, and contains two hypermodified nucleosides--3 -3(3-amino-3-carboxylpropyl)uridine (acp3U) and beta-D-galactosylqueuosine (Q*). The molecule also has a pseudouridine in the middle position of the anticodon, and is the first tRNA sequenced which has an adjacent pair of N2,N2-dimethylguanosine (m22G) residues.     

The nucleotide sequence of a major species of leucine tRNA from bovine liver.

Through the use of a variety of post-labeling techniques, the nucleotide sequence of a major species of leucine tRNA from bovine liver was determined to be pG-G-U-A-G-C-G-U-G-m-G-C-ac-C-G-A-G-C-G-G-D-C-psi-A-A-G-G-C-m-G-C-U-G-G-A-psim- U-I-A-G-m-G-C-psi-C-C-A-G-U-C-psi-C-psi-U-C-G-G-G-G-G-m-C-G-U-G-G-G-T-psi-C-G-m -A-A-U-C-C-C-A-C-C-G-C-U-G-C-C-A-C-C-AOH. A comparison of known sequences of leucine tRNAs shows a consistent set of features which clearly distinguish prokaryotic and eukaryotic leucine tRNAs from each other.     

The nucleotide sequence of rat liver tRNAAsn

The major species of asparagine specific tRNA was isolated from rat liver, degraded to oligonucleotides, and shown to have the nucleotide sequence pG-U-C-U-C-U-G-U-m¹G-m²G-C-G-C- A-A-D-C-G-G-D-X-A-G-C-G-C-m²G-ψ-ψ-C-G-G-C-U-Q-U-U-t⁶A-A-C-C-G- A-A-A-G-m⁷G-D-U-G-G-U-G-G-Z-ψ-C-G-m¹A-G-C-C-C-A-C-C-C-A-G-G-G- A-C-G-C-C-A_OH. Although this tRNA contains several modified nucleotides in their expected positions, it is unique in having X, 3-(3-Amino-3-carboxy-n-propyl)uridine in loop I rather than in loop III; Q, 7-(4,5-cis-dihydroxyl-1-cyclopenten-3-yl-aminomethyl)-7-deazaguanosine in the wobble position of loop II; and Z, an unknown, and presently uncharacterized nucleoside, at position 23 from the 3′ terminus usually occupied by ribothymidine.     

The nucleotide sequence of a glutamine tRNA from rat liver.

A glutamate tRNA from rat liver was purified. By means of post-labeling techniques, its nucleotide sequence was shown to be: pU-C-C-C-A-C-A-U-m1G-G-U-C-psi-A-G-C- G-G-D-D-A-G-G-A-U-U-C-C-U-G-G-psi-U-mcm5S2U-U-C-A-C-C-C-A-G-G-C-G- G-C-m5C-m5C-G-G-G-Tm-psi-C-G-A-C-U-C-C-C-G-G-U-G-U-G-G-G-A-A-C-C-AOH. The sequence is remarkably similar to that of tRNAGlu from Drosophila melanogaster. Only 10 out of 75 nucleotides in the two tRNAs are different.     

The nucleotide sequence of a major glutamine tRNA from rat liver

A major glutamine tRNA from rat liver was purified. Post-labeling techniques showed its nucleotide sequence to be: pG-G-U-U-C-C-A-U-m(1)G-G-U-G-psi-A-A-D-Gm-G-D-D-A-G-C-A-C-U-C-U-G-G-A-Cm-U-C-U-G-A-A-psi-C-C-A-G-C-G-A-U-m(5)C-m(5)C-G-A-G-psi-psi-C-A-m(1)A-A-U-C-U-C-G-G-U-G-G-A-A-C-C-U-C-C-A(OH).Images     

The nucleotide sequence of a glutamate tRNA from rat liver.

A glutamate tRNA from rat liver was purified. By means of post-labeling techniques, its nucleotide sequence was shown to be: pU-C-C-C-A-C-A-U-m1G-G-U-C-psi-A-G-C- G-G-D-D-A-G-G-A-U-U-C-C-U-G-G-psi-U-mcm5s2U-U-C-A-C-C-C-A-G-G-C-G- G-C-m5C-m5C-G-G-G-Tm-psi-C-G-A-C-U-C-C-C-G-G-U-G-U-G-G-G-A-A-C-C-AOH. The sequence is remarkably similar to that of tRNA4Glu from Drosophila melanogaster. Only 10 out of 75 nucleotides in the two tRNAs are different.     

The nucleotide sequence of rabbit liver transferrin cDNA

The cDNA sequence of rabbit liver transferrin has been determined. The largest cDNA was 2279 base pairs (bp) in size and encoded 694 amino acids consisting of a putative 19 amino acid signal peptide and 675 amino acids of plasma transferrin. The deduced amino acid sequence of rabbit liver transferrin shares 78.5% identity with human liver transferrin and 69.1% and 44.8% identity with porcine and Xenopus transferrins, respectively. At the amino acid level, vertebrate transferrins share 26.4% identity and 56.5% similarity. The most conserved regions correspond to the iron ligands and the anion binding region. Optimal alignment of transferrin sequences required the insertion of a number of gaps in the region corresponding to the N-lobe. In addition, the N-lobes of transferrins share less amino acid sequence similarity than the C-lobes.     

The nucleotide sequence of bovine MHC class IIDQB andDRB genes

The nucleotide sequences of most of the exons and parts of the introns of twoBoLA-DQB genes and twoBoLA-DRB genes have been determined. The structure of these genes is very similar to that of human major histocompatibility complex (MHC) class II genes. The twoDQB genes probably represent true alleles. Based on the exons sequenced, bothDQB genes and one of theDRB genes seem to be functional. The otherDRB gene is a pseudogene; stopcodons are found in the exons encoding the second and transmembrane domain and, furthermore, a 2 base pair (bp) deletion has occured in the leader exon which places the initiation start codon out of frame. Also in this pseudogene, an almost perfect inverted repeat of 200 bp is found flanking the exon encoding the first domain, which might have been the result of a duplication/inversion event. The sequences presented in this paper do not contain any repetitions. Therefore, DNA fragments containing these sequences can be used as homologous bovine probes in restriction fragment length polymorphism (RFLP) analysis to study disease association in cattle.The nucleotide sequence data reported in this paper have been submitted to the GenBank nucleotide sequence database and have been assigned the accession numbers M30002–M30014. Address correspondence and offprint requests to: M. A. M. Groenen.     

The nucleotide sequence of rat liver glycogen phosphorylase cDNA.

The nucleotide sequence of a cDNA coding for rat liver glycogen phosphorylase has been determined. The 2715 base pairs of the cDNA are sufficient to encode the total protein as determined by comparison with the liver type of glycogen phosphorylase of man. Human and rat liver glycogen phosphorylase showed 86% homology at the DNA level whereas the deduced amino acid sequence has 93.5% identity.     

The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase

The data upon which the sequence of the 506 residues in the subunit of bovine liver catalase (BLC) is based are presented in detail. A partial sequence of bovine erythrocyte catalase (BEC) which accounts for 493 residues shows complete concordance with the BLC data. On the other hand, BEC has at least 517 residues, that is, an extension beyond the C terminus of the BLC data. Although normally BLC has only 506 residues, there is evidence that, at some point in its history, it also had the C-terminal extension. It is speculated that this extension is lost in BLC either through a different processing of the molecule in liver than in erythrocytes or by partial degradation in the first stages of catabolism.     

The complete nucleotide sequence of human liver cytochrome b5 mRNA

We have isolated and sequenced a cDNA clone corresponding to human liver cytochrome b5 mRNA. The 760 base pair (bp) sequence contains the complete coding and 3' non-translated regions plus 52 bp of 5' non-translated sequence. The derived amino acid sequence showed that the previous assignment of several amino acids was in error. In addition, the sequence of the previously unknown COOH hydrophobic region has been obtained.     

Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of beta-subunit and nucleotide sequence of corresponding cDNA

Primary structure of beta-subunit of the cyclic GMP phosphodiesterase has been determined by the parallel analysis of the protein amino acid sequence and the corresponding cDNA nucleotide sequence. The beta-subunit contains 852 amino acid residues, its molecular mass is 98291 Da. A significant homology is found between beta- and alpha-subunit of the cGMP phosphodiesterase.     

Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase from bovine heart

The complete amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase (cGS-PDE) of bovine heart has been determined by analysis of five digests of the protein; placement of the C-terminal 330 residues has been confirmed by interpretation of the corresponding partial cDNA clone. The holoenzyme is a homodimer of two identical N alpha-acetylated polypeptide chains of 921 residues, each with a calculated molecular weight of 103,244. The C-terminal region, residues 613-871, of the cGS-PDE comprises a catalytic domain that is conserved in all phosphodiesterase sequences except those of PDE 1 from Saccharomyces cerevisiae and a secreted PDE from Dictyostelium. A second conserved region, residues 209-567, is homologous to corresponding regions of the alpha and alpha' subunits of the photoreceptor phosphodiesterases. This conserved domain specifically binds cGMP and is involved in the allosteric regulation of the cGS-PDE. This regulatory domain contains two tandem, internal repeats, suggesting that it evolved from an ancestral gene duplication. Common cyclic nucleotide binding properties and a distant structural relationship provide evidence that the catalytic and regulatory domains within the cGS- and photoreceptor PDEs are also related by an ancient internal gene duplication.