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At least 703 records · Page 39Linked to original sources
PubMed1995

[The 5'-region of mink ribosomal protein S26 cDNA: sequencing and comparative analysis].

The 5'-terminal region of the mink S26 ribosomal protein cDNA was cloned using polymerase chain reaction. The nucleotide sequences of the 5'-UTR (24 bp) and a 120-bp fragment of the coding region of RPS26 mRNA were determined. The homology between the coding regions of the human and mink RPS26 mRNAs proved to be 90.8%. The nucleotide sequences of the 5'-UTRs of mink, human, and rat RPS26 mRNAs, as well as mRNAs of the Drosophila S31 protein and Neurospora crp-5 protein, which are homologous to mammalian RPS26, were compared. A highly conserved 9-bp sequence located immediately upstream of the AUG codon was revealed in the 5'-UTR of the RPS26 mRNAs from different species.

Animals↗
PubMed1992

cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils.

The full-length cDNA of a neutrophil antibiotic dodecapeptide has been cloned by reverse transcription/PCR from bovine bone marrow RNA. This peptide was originally isolated from bovine neutrophils, and shown to exert a potent antimicrobial activity in vitro on both Escherichia coli and Staphylococcus aureus. The cDNA codes for a polypeptide of 155 amino acid residues with a predicted mass of 17,629 Da and a pI of 8.03. The deduced sequence comprises a putative signal peptide of 29 amino acids, a 114 residue pro-region, and a carboxy-terminal dodecapeptide corresponding to the mature antibiotic. The pro-sequence displays extensive identity to corresponding regions of other structurally unrelated antibiotic peptides of bovine neutrophils recently cloned.

Amino Acid Sequence↗
PubMed1995

Salmon HNF1: cDNA sequence, evolution, tissue specificity and binding to the salmon serum albumin promoter.

cDNA clones coding for the transcription factor HNF1 have been isolated from Atlantic salmon (Salmo salar L.). The 559 amino acid residue long encoded protein shows high conservation, with respect to other species, of the domains necessary for DNA-binding: the HNF1 atypical homeodomain, the POU related sequence and the dimerisation domain. Alignment with rat HNF1 protein reveals that the transcription activation domains ADI and ADIII are relatively conserved in the fish sequence whereas ADII is not. Phylogenetic analysis indicates that higher vertebrate HNF1s and the related variant HNF1s (vHNF1s) are more closely related to each other than any of them is to Salmon HNF1, suggesting that the duplication event from which HNF1 and vHNF1 genes arose occurred after the divergence of the tetrapod and teleost ancestors. Northern blot analysis show a single transcript, of about 2.6 kb, which is not exclusive to liver but is also present in intestine, kidney and spleen. Using polymerase chain reaction (PCR) we have isolated the salmon albumin gene promoter which contains, upstream of the TATA box, a potential binding site for HNF1. The salmon HNF1 protein synthesized by in vitro transcription-translation of the full-length cDNA is able to bind specifically with equivalent affinities to either the rat or salmon albumin promoter.

Amino Acid Sequence↗
PubMed1985

Use of the deoxyinosine-containing probe to isolate and sequence cDNA encoding the fusion (F) glycoprotein of Sendai virus (HVJ).

A synthetic 20-mer based on the known amino acid (aa) sequence of the N-terminus of Sendai virus F1 polypeptide was synthesized. Using this dI-probe, which contained deoxyinosines at all six ambiguous codon positions, we isolated clones carrying cDNAs for the F mRNA of Sendai virus. Nucleotide (nt) sequence analysis revealed a long open reading frame (ORF) that encodes a protein of 565 aa. Thus, this type of dI-probes should prove useful for selecting cDNA clones, when the aa sequence is known and is characterized by high codon redundancy.

Amino Acid Sequence↗
PubMed1997

cDNA sequence analysis of a novel neurotoxin homolog from Taiwan banded krait.

The cDNA encoding a novel protein was constructed from the cellular RNA isolated from the venom glands of Bungarus multicinctus (Taiwan banded krait) by reverse transcription-polymerase chain reaction. The deduced amino acid sequence of this novel protein contains 68 amino acid residues with 10 cysteine residues. Comparative sequence analyses show that it is structurally related to alpha-bungarotoxin and kappa-bungarotoxins from Bungarus multicinctus venom. Eight out of the ten cysteine residues in this protein are located at the homologous positions as those in the neurotoxins. However, instead of the fifth disulfide linkage appearing in loop II of alpha-bungarotoxin and kappa-bungarotoxins, the other two cysteine residues in this novel toxin are situated at the N-terminal region. Phylogenetic analyses suggest that it probably represents a small evolutionary divergence between the long and short neurotoxins.

Amino Acid Sequence↗
PubMed1988

cDNA sequence and predicted primary structure of the gamma subunit from the ATP synthase from Chlamydomonas reinhardtii.

The 1701-base nucleotide sequence (not including the poly(A) tail) of a cDNA for the gamma subunit of the ATP synthase from Chlamydomonas reinhardtii was determined. A start translation sequence, 23 bases in from the 5' end, initiates an 1074-base-long open reading frame. The sequence of the first 21 amino acids at the amino-terminal end of the mature gamma subunit from C. reinhardtii was determined and compared to the deduced amino acid sequence of the open reading frame. From this it was determined that the mature protein contains 323 amino acids, with the first 35 amino acids probably being part of the transit peptide. The length of the mature protein is the same as that for the mature gamma subunit from spinach, for which only a few of the amino acids of the transit peptide are known. The similarity of the two mature proteins at the nucleotide level is 56% while at the amino acid level it is 77%. In addition, the 3 cysteines, which in spinach are involved in the energy-linked catalytic functions of the ATP synthase, are conserved in the predicted amino acid sequence for the gamma subunit from C. reinhardtii. In contrast, the mature C. reinhardtii gamma subunit contains 3 additional cysteine residues not found in the spinach gamma subunit.

Amino Acid Sequence↗
PubMed1988

cDNA sequence of the beta 2-subunit of human liver alcohol dehydrogenase.

A cDNA library of mRNA from a human liver expressing the beta 2-subunit of alcohol dehydrogenase was constructed in lambda gt11. One clone coding for 352 of a total of 374 amino acid residues of the beta 2-subunit was isolated. The sequence differed from that of the beta 1-subunit at one nucleotide position resulting in an Arg/His exchange at position 47 of the peptide chain, in agreement with data from protein sequence analysis [(1984) FEBS Lett. 173, 360-366].

Alcohol Dehydrogenase↗
PubMed2004

Crassostrea gigas ferritin: cDNA sequence analysis for two heavy chain type subunits and protein purification.

Ferritin has been shown as being the principal iron storage in the majority of living organisms. In marine species, ferritin is also involved in high-level accumulation of (210)Po. As part of our work on the investigation of these radionuclides' concentration in natural environment, ferritin was searched at the gene and protein level. Ferritin was purified from the visceral mass of the oyster Crassostrea gigas by ion-exchange chromatography and HPLC. SDS-PAGE revealed one band of 20 kDa. An Expressed Sequence Tag (EST) library was screened and led to the identification of two complementary DNA (cDNA) involved in ferritin subunit expression. The complete coding sequences and the untranslated regions (UTRs) of the two genes were obtained and a 5' Rapid Amplification of cDNA Ends (RACE) was used to obtain the two iron-responsive elements (IREs) with the predicted stem-loop structures usually present in the 5'-UTR of ferritin mRNA. Sequence alignment in amino acid of the two new cDNA showed an identity with Pinctada fucata (85.4-88.3%), Lymnaea stagnalis (79.3-82.2%) and Helix pomatia (79.1-79.1%). The residues responsible for the ferroxidase center, conserved in all vertebrate H-ferritins, are present in the two oyster ferritin subunits. Oyster ferritins do not present the special characteristics of other invertebrate ferritins like insect ferritins but have some functional similarities with the vertebrate H chains ferritin.

Amino Acid Sequence↗
PubMed1998

cDNA sequence and deduced amino acid sequence of bovine oviductal fluid catalase.

A bovine oviductal fluid catalase (OFC) which preferentially binds to the acrosome surface of some mammalian spermatozoa has recently been purified. The objectives of this study were to clone the OFC, obtain the full-length cDNA and protein sequence and determine which characteristics of the proteins are associated with the binding of the enzyme to sperm surface. Northern blot analysis revealed low levels of catalase mRNA in bovine oviducts and uterus compared to the liver and kidney. Screening of a cDNA library from the cow oviduct permit to obtain a full-length cDNA of 2282 bp, with an open reading frame of 1581 bp coding for a deduced protein of 526 amino acids (59,789 Da). The deduced protein contained four potential N-glycosylation sites and many potential O-glycosylation sites. The OFC protein exhibited high identity with catalase from other bovine tissues, likewise with catalases from human fibroblast and kidney, and with rat liver catalase. The homology of amino acid sequence of OFC with bovine liver catalase was about 99%. However the OFC possess an extended carboxyl terminus of 20 amino acids not present on the liver catalase. This result is supported by a lower mobility of the OFC compared to the liver catalase when both proteins are submitted on SDS-PAGE.

Amino Acid Sequence↗
PubMed1999

cDNA sequence analysis of a novel member of the three loop protein family from the Chinese continental banded krait.

The cDNA encoding a novel three loop protein was cloned from cellular RNA isolated from the venom gland of Bungarus multicinctus multicinctus by RT-PCR. The mature protein has 82 amino acid residues. It shared only 25-38% similarity with some cardiotoxins and did not have sequence similarity with neurotoxins, while its cDNA was about 70% similar to both the cDNAs encoding neurotoxins and the cDNAs encoding cardiotoxins.

Amino Acid Sequence↗
PubMed1994

The cDNA sequence of beef heart CII-3, a membrane-intrinsic subunit of succinate-ubiquinone oxidoreductase.

We provide the first full-length cDNA and amino acid sequences for beef heart CII-3, one of two hydrophobic subunits that bind succinate dehydrogenase to the mitochondrial inner membrane to form succinate-ubiquinone oxidoreductase (EC 1.3.99.1). Other low molecular weight proteins present in preparations of the isolated complex, including three possible forms of the second anchor polypeptide CII-4, have been identified by amino terminal sequencing.

Amino Acid Sequence↗
PubMed1982

Rat beta casein cDNA: sequence analysis and evolutionary comparisons.

The complete sequence of a 1072 nucleotide rat beta-casein cDNA insertion in the hybrid plasmid pC beta 23 has been determined. Primer extension was employed to determine the sequence of an additional 82 5'-terminal nucleotides in beta-casein mRNA. Rat beta-casein mRNA consists of a 696 nucleotide coding region, flanked by 52 nucleotide 5' and 406 nucleotide 3' noncoding regions, including a 40 nucleotide poly(A) tail. The derived 216 amino acid sequence of rat beta-casein was compared to the previously determined sequences of beta-caseins from several other species. Approximately 38% of the amino acids have been conserved among the rat, ovine, bovine and human sequences and these conserved amino acids occurred in clusters throughout the protein. One such cluster containing the majority of the potential casein phosphorylation sites was located near the amino terminus. Contrary to the considerable divergence observed for the processed beta-casein, 14 of 15 amino acids in the signal peptide sequence of the precasein were identical between the rat and ovine caseins.

Amino Acid Sequence↗
PubMed1996

Carp cDNA sequence encoding a putative diazepam-binding inhibitor/endozepine/acyl-CoA-binding protein.

A full-length cDNA coding for common carp diazepam-binding inhibitor (DBI)/endozepine (EP)/acyl-CoA-binding protein (ACBP) was isolated and sequenced. The deduced DBI/EP/ACBP is comprised of 87 amino acids (including initiating methionine) without possessing a signal peptide. Common carp DBI/EP/ACBP displays 77%, 78%, 70%, 63%, 61% and 45% identity with human, bovine, rat, frog, duck and yeast DBI/EP/ACBP, respectively.

Acyl Coenzyme A↗
PubMed2004

Combining transcriptome data with genomic and cDNA sequence alignments to make confident functional assignments for Aspergillus nidulans genes.

Whole genome sequencing of several filamentous ascomycetes is complete or in progress; these species, such as Aspergillus nidulans, are relatives of Saccharomyces cerevisiae. However, their genomes are much larger and their gene structure more complex, with genes often containing multiple introns. Automated annotation programs can quickly identify open reading frames for hypothetical genes, many of which will be conserved across large evolutionary distances, but further information is required to confirm functional assignments. We describe a comparative and functional genomics approach using sequence alignments and gene expression data to predict the function of Aspergillus nidulans genes. By highlighting examples of discrepancies between the automated genome annotation and cDNA or EST sequencing, we demonstrate that the greater complexity of gene structure in filamentous fungi demands independent data on gene expression and the gene sequence be used to make confident functional assignments.

Aspergillus nidulans↗
PubMed1991

cDNA sequence of the long mRNA for human glutamine synthase.

Screening a human liver cDNA library in lambda ZAP revealed several clones for the mRNA of glutamine synthase. The longest clone was completely sequenced and consists of a 109 bp 5' untranslated region, a 1119 bp protein coding region, a 1498 bp 3' untranslated region and a poly(A) tract of 12 bp.

Base Sequence↗
PubMed1994

Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization.

Here we describe the molecular cloning of 7.1-kilobase cDNA encoding chick cardiac muscle tensin. It contains an open reading frame of 1,744 amino acid (aa) residues. Sequence analysis reveals that, in addition to the previously noted SH2 domain (Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B. J., Roberts, T. M., An, Q., and Chen, L. B. (1991) Science 252, 712-715), tensin contains virtually all of the known sequence (362 aa) of insertin, an actin-capping protein that allows actin monomer to be "inserted" (Schroer, E., and Wegner, A. (1985) Eur. J. Biochem. 153, 515-520). Moreover, tensin shares partial homology with actin (46.7% identity in 30 aa), beta-spectrin's actin-binding consensus (40% identity in 26 aa), BCR (40% identity in 25 aa), catenin alpha (35% identity in 45 aa), synapsin Ia (25.6% identity in 156 aa), IL-3 receptor (20.2% identity in 384 aa), and IL-2/EPO receptors (14% identity in 20 aa). Recombinant full-length tensin, tagged with an influenza-derived epitope, was over-expressed by a baculovirus system and purified to apparent homogeneity. It migrates as a 200-kDa protein in SDS-polyacrylamide gel electrophoresis, similar to the native tensin. The structure of the tensin molecule has been characterized by light scattering, electron microscopy, and gel filtration. Nine monoclonal antibodies recognizing different regions of tensin have been prepared and characterized. The epitope-tagged recombinant tensin gene was subcloned into a pRcCMV vector and transfected into NIH 3T3 cells. Immunofluorescence stainings with monoclonal antibodies specific for chick tensin (not cross-reactive with mouse tensin) showed that the expressed protein is indeed localized at focal contacts, as that of native tensin.

3T3 Cells↗
PubMed1992

cDNA sequence of a second fibrinogen alpha chain in lamprey: an archetypal version alignable with full-length beta and gamma chains.

The message for a second fibrinogen alpha chain has been cloned from a lamprey liver cDNA library. The sequence is unique in that the amino-terminal half is homologous to all other known alpha chains, including another from lamprey, but its carboxyl-terminal half is homologous to the carboxyl-terminal portions of beta and gamma chains, segments that compose the distal globular regions of fibrinogen. The structural pattern of this newly discovered alpha chain suggests that it could be a direct descendant of the archetypal chain that existed prior to the gene duplications that led to unique beta and gamma chains and before the dislocating events that gave rise to contemporary alpha chains.

Amino Acid Sequence↗
PubMed1990

Human epithelial tumor antigen cDNA sequences. Differential splicing may generate multiple protein forms.

The isolation and characterization of complementary DNAs (cDNAs) which code for an epithelial antigen aberrantly expressed in human breast tumor tissue are described here. The only information regarding the primary structure of this potentially important antigen has been a 20-amino-acid repeat motif. We now report the complete amino acid sequences of different forms of the human epithelial tumor antigen as deduced from the nucleotide sequence of isolated non-repeat cDNAs. The diversity of protein forms is generated by a series of alternative splicing events that occur in the regions located upstream and downstream to a central tandem repeat array. Isolated cDNAs coding for the upstream region show that differential usage of alternative splice acceptor sites may generate two protein forms containing putative signal peptides of varying hydrophobicities. The complexity of possible antigen forms is further compounded by alternative splicing events occurring in the region 3' to the repeat array. The isolated cDNAs 3' to the tandem repeats indicate that whereas one mRNA transcript is colinear with the gene, and defines an open reading frame (ORF) containing 160 amino acids downstream to the repeat array, a second cDNA correlates with a mRNA that is generated by a series of splicing events. The deduced amino acid sequence of the spliced cDNA contains an ORF that is identical for 149 amino acids downstream to the repeat array with the amino acid sequence of the unspliced cDNA. At this point it diverges and continues for an additional 179 amino acids. The sequence contains a highly hydrophobic 28-amino-acid peptide, located towards the carboxyl terminus, that may correspond to a transmembrane region. The cDNAs and deduced amino acid sequences, presented here, define the complete amino acid sequences of the epithelial tumor antigen and demonstrate the existence of multiple protein forms that probably localize to different cellular and extracellular compartments.

Amino Acid Sequence↗