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Results for “cDNA sequencing”

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At least 1,261 records · Page 70Linked to original sources
PubMed1989

Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats.

In the rat, a cytosolic isozyme of aldehyde dehydrogenase, designated ALDH-PB, can be induced in the liver by administration of phenobarbital (PB). ALDH-PB activity and mRNA are induced in Long-Evans rats that possess a responsive (R) allele but are not induced in homozygous nonresponsive rats (rr), although the rr genotype is competent to induce other PB-responsive mRNAs. ALDH-PB mRNA is expressed in the basal state (without PB administration) in hepatic tissue in both RR and rr genotypes. We report the complete nucleotide sequence of the rat ALDH-PB mRNA. The protein encoded by the ALDH-PB mRNA is 501 amino acids in length and has a predicted molecular mass of 54,540 daltons. The amino acid sequence predicted from the mRNA demonstrates a strong conservation between the rat ALDH-PB and the human cytosolic aldehyde dehydrogenase hALDH-1. We demonstrate the ALDH-PB, cytochrome P-450b, cytochrome P-450e, and glutathione S-transferase Ya subunit mRNA levels in the liver are altered noncoordinately by administration of PB in RR and rr genotypes. The strikingly different responses to PB administration between the various mRNA species in each of the genotypes suggest that the regulation of specific gene expression by PB may involve multiple pathways.

Aldehyde Dehydrogenase↗
PubMed1988

Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence.

The complete amino acid sequence of acetyl-CoA carboxylase from chicken liver has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA. The results were confirmed by Edman degradation of peptide fragments obtained by digestion of the enzyme polypeptide with Achromobacter proteinase I or staphylococcal serine proteinase. Chicken liver acetyl-CoA carboxylase is predicted to be composed of 2,324 amino acid residues, having a calculated molecular weight of 262,706. The biotin carboxyl carrier protein domain is located in the middle region of the enzyme polypeptide. The amino-terminal portion of the acetyl-CoA carboxylase has been found to exhibit a homologous primary structure to that of carbamyl phosphate synthetase. Localization of possible functional domains including biotin carboxylase subsite in the acetyl-CoA carboxylase polypeptide is discussed.

Acetyl-CoA Carboxylase↗
PubMed1989

Polypeptide structure of germin as deduced from cDNA sequencing.

Synthesis of a relatively rare glycoprotein (germin) signals the onset of growth in germinating wheat embryos. Germin mRNA (1075 nucleotide residues) has an 85-residue 5'-untranslated sequence, a 69-residue sequence that can encode a 23-residue signal-peptide sequence, a 603-residue sequence that can encode a 201-residue mature-protein sequence, and a 318-residue 3'-untranslated sequence that begins with a UAA-terminator codon, ends with a 63-residue polyadenylate tract, and has three polyadenylation (and other, related) signals (AAUAAN etc.). One polyadenylation signal is just 9 nucleotides from the polyadenylation site, the shortest stretch of nucleotides yet found between polyadenylation signal and site in any animal or plant mRNA. The mature-protein coding sequence in germin mRNA contains an unusually high proportion (87%) of G + C in the third positions of its codons. The amino acid sequence of germin does not have extensive internal homologies or repetitions, and it is not characterized by regions of unusually high charge density, as is nucleoplasmin, another water-soluble homopentameric protein with otherwise closely related structural properties. Germin does, however, contain a stretch of 34 uncharged amino acid residues and these may possibly mediate its homopentameric structure and its remarkable resistance to enzymic proteolysis. In view of a possible association of germin with cellular membranes, the most interesting relatedness of the germin sequence to the sequences of other proteins is an 80% homology between a decapeptide sequence in mature germin and a decapeptide sequence in Escherichia coli glycerol-3-phosphate acyltransferase. The relation of germin-gene structure to overall gene regulation during early plant growth is discussed.

Amino Acid Sequence↗
PubMed1995

Identification of cDNA sequences by specific oligonucleotide sets. Computer tool and application.

A computer tool has been developed for revealing sets of oligonucleotides invariant for isofunctional families of DNA (RNA) and for using these in functional identification of nucleotide sequences. The tool allows one to: build up vocabularies of invariant oligonucleotides for the families of isofunctional nucleotide sequences; assess significance of the vocabularies; identify nucleotide sequences with the vocabularies of invariant oligonucleotides; determine the most effective identification parameters to minimize first and second type errors; assess the efficiency of identification of individual isofunctional families with the oligonucleotide vocabularies; determine the evolutionary characteristics of the families of isofunctional sequences on which vocabulary volume depends. Based on the system mentioned, we have analyzed a total of 322 protein-encoding gene families and have built up sets of invariant oligonucleotides, or again, oligonucleotide vocabularies that are characteristic of gene families and subfamilies. Identification of nucleotide sequences belonging to these families with the sets of invariant oligonucleotides revealed has been shown. Under the most effective identification parameters, the first type error (false negative) on control (independent) data was 10-15%, the second type error (false positive) was just 1-2 redundant sequences per sequence being examined. As has been shown, the volume of a vocabulary of invariant oligonucleotides depends on the percentage of variable positions in the multiple alignment within a family.

Base Sequence↗
PubMed1994

cDNA sequences of Schistosoma japonicum coding for two cathepsin B-like proteins and Sj32.

Sequences of three cDNAs of Schistosoma japonicum are presented. Two of them code for the antigens Sj32 (hemoglobinase) and cathepsin B. The third clone represents a mutant derivative of the cathepsin B gene. The DNA and amino acid sequences are compared to their homologues from S. mansoni. The mutant cathepsin B, in which the Cys29 in the active center is replaced by Ser, is discussed with respect to a possible function.

Amino Acid Sequence↗
PubMed1993

Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a novel class of glycosyltransferase that mediates molecular grafting between matrix polysaccharides in plant cell walls.

Endoxyloglucan transferase is a novel class of glycosyltransferase recently purified from Vigna angularis (Nishitani, K,, and Tominaga, R. (1992) J. Biol. Chem. 267, 21058-21064). This enzyme is the first transferase identified that catalyzes molecular grafting between polysaccharide cross-links in the cell wall matrix and participates in reconstruction of the network structure in the cell wall. Based on the NH2-terminal amino acid sequence information of the purified transferase, we have here cloned and sequenced cDNAs derived from five different plant species, V. angularis, Triticum aestivum, Arabidopsis thaliana, Lycopersicon esculentum, and Glycine max. In the five plant species, the amino acid sequence of the mature proteins is conserved in the range of 71-90% throughout their length. The consensus sequence for N-linked glycosylation, and four cysteine residues are all conserved in the five species. Thus, the endoxyloglucan transferase protein is ubiquitous among higher plants. The highly conserved DNA sequence will serve as a promising tool for exploring the molecular process by which cell wall construction, and hence cell growth, is regulated.

Amino Acid Sequence↗
PubMed1993

Cloning of cDNA sequences encoding human alpha 2 and alpha 3 gamma-aminobutyric acidA receptor subunits and characterization of the benzodiazepine pharmacology of recombinant alpha 1-, alpha 2-, alpha 3-, and alpha 5-containing human gamma-aminobutyric acidA receptors.

cDNAs encoding human alpha 2 and alpha 3 gamma-aminobutyric acidA receptor subunits have been cloned. Their deduced amino acid sequences show much sequence identity with the published bovine sequences (98.2% and 97.0% for alpha 2 and alpha 3, respectively). Human alpha 1 beta 1 gamma 2, alpha 2 beta 1 gamma 2, alpha 3 beta 1 gamma 2, and alpha 5 beta 1 gamma 2 subunit combinations were expressed in transiently transfected cells and their pharmacologies were characterized using a series of benzodiazepine (BZ) binding site ligands. Human alpha 1-containing receptors exhibited a BZ1-type pharmacology, and alpha 2-, alpha 3-, and alpha 5-containing receptors exhibited a broadly BZ2-type pharmacology. The partial inverse agonist Ro15-4513 showed an approximately 10-15-fold higher affinity for alpha 5-containing than for alpha 1-, alpha 2-, or alpha 3-containing receptors and is thus the first compound shown to have a significantly higher affinity for another receptor subtype than for alpha 1 beta 1 gamma 2.

Amino Acid Sequence↗
PubMed1998

A monophyletic origin of heart-predominant lactate dehydrogenase (LDH) isozymes of gnathostome vertebrates: evidence from the cDNA sequence of the spiny dogfish (Squalus acanthias) LDH-B.

Duplication of a single lactate dehydrogenase locus early in vertebrate evolution has been proposed to have given rise to Ldh-A and Ldh-B, the encoded isozymes of which predominate in skeletal and heart muscle, respectively. This view has been challenged recently by phylogenetic analyses of LDH sequences. One question that has been raised is whether the heart-predominant isozyme (LDH-B) of cartilaginous fishes is orthologous to that of bony fishes and their derivatives. To address this issue, we determined the complementary DNA sequence of the LDH-B of the chondrichthyan Squalus acanthias. Phylogenetic analysis of this and other LDH isozyme sequences provided strong support for a single origin of LDH-Bs prior to the divergence of cartilaginous and bony fishes.

Amino Acid Sequence↗