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At least 1,333 records · Page 74Linked to original sources
PubMed1990

Partial amino acid sequence of the major intrinsic protein (MIP) of the chicken lens deduced from the nucleotide sequence of a cDNA clone.

A cDNA clone of the major intrinsic protein (MIP) of the chicken lens was isolated. This clone covers the C-terminal half of the coding region and 3'-untranslated region including a polyadenylation signal. Comparison with the bovine MIP cDNA sequence revealed that: (1) the amphilphilic transmembrane helix in bovine MIP is highly hydrophobic in chicken MIP, and is thus unlikely to offer a hydrophilic lining of the transmembrane pore, and (2) the possible calmodulin binding site is conserved especially at amino acid residues which are postulated to be important in its binding with calmodulin. Northern blotting revealed the presence of transcripts of different lengths, two of which correspond closely to the transcripts of bovine MIP.

Amino Acid Sequence↗
PubMed1989

Cloning and sequencing of a cDNA encoding the precursor to the 24 kDa iron-sulfur protein of human mitochondrial NADH dehydrogenase.

1. We have isolated a cDNA encoding the 24 kDa subunit, an iron-sulfur protein, of mitochondrial NADH dehydrogenase from a human fibroblast cDNA library by colony hybridization using a rat 24 kDa subunit cDNA as a probe. 2. The presequence predicted from the human cDNA sequence is typical of precursors to mitochondrial proteins in a high content of basic residues and in the absence of acidic ones. 3. The mature form of the human 24 kDa subunit shows 95% homology with its rat counterpart. Five cysteine residues are conserved among human, rat and bovine; four of these are expected to be involved in the binding of a binuclear iron-sulfur cluster.

Amino Acid Sequence↗
PubMed1992

Nucleotide sequence of a cDNA from Onchocerca gibsoni encoding a novel repetitive antigen.

mRNA from uterine microfilariae of the cattle parasite Onchocerca gibsoni was used for the construction of cDNA libraries. A cDNA clone encoding an antigen recognized by serum from human individuals infected with O. volvulus was found to contain five copies of an 87 bp unit. These 87 bp units were present in the genome in high copy number as long tandem arrays. These are the first cDNA sequence data obtained directly from larvae of any Onchocerca species.

Amino Acid Sequence↗
PubMed1986

Bovine interstitial retinol-binding protein (IRBP)--isolation and sequence analysis of cDNA clones, characterization and in vitro translation of mRNA.

Three clones for b-IRBP were isolated by anti b-IRBP screening of two bovine retina libraries in the expression vector lambda gt11. The cDNA inserts were then used as hybridization probes to screen and isolate three more clones in a bovine retina library in the non-expression vector lambda gt10. The six overlapping clones generated a b-IRBP cDNA sequence of 3400 nucleotides. An open reading frame encoded the complete amino acid sequences of 8 of the 35 b-IRBP tryptic peptides purified in the present study. One tentative glycosylation site was identified. The coding region was followed by TAG translation terminating codon and an untranslated stretch of about 1700 nucleotides that ended in a sequence containing a presumptive AATAAA polyadenylation signal that was 18 nucleotides upstream from a 10 nucleotide oligo(A) tract. The coding region for b-IRBP would be expected to be 3300 bp long, but Northern blot hybridization experiments performed with bovine retina polyadenylated RNA and probes containing part of the coding region established that the mRNA for b-IRBP consisted of a major species of about 6300 bp, and a minor species of 5200 bp. In vitro translation of bovine retina polyadenylated RNA in a rabbit reticulocyte lysate system yielded an immunoreactive protein that was comparable in size with nonglycosylated, mature IRBP, showing that it is not synthesized from a large precursor, and supporting our finding that the mRNA contains an extensive non-coding region.

Amino Acid Sequence↗
PubMed1993

Nucleotide sequence of the cDNA encoding nucleoside diphosphate kinase II from spinach leaves.

The primary structure of nucleoside diphosphate (NDP) kinase II, one of the two isozymes found in spinach leaves, has been deduced from its cDNA sequence. NDP kinase II comprises 233 amino acid residues and has a molecular mass of 26,107 Da, which is larger than that of the purified NDP kinase II subunits (18 kDa) by about 8 kDa, suggesting that NDP kinase II might be post-translationally processed. Homology was found between the sequence of spinach NDP kinase II, and the sequences of spinach NDP kinase I, rat NDP kinases alpha and beta, Dictyostelium discoideum NDP kinase, the human Nm23-H1 and Nm23-H2 proteins and the awd protein of Drosophila melanogaster.

Amino Acid Sequence↗
PubMed1994

Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins.

We have determined the cDNA sequence encoding a 154 amino acid human Id-1 helix-loop-helix protein. Comparison with the amino acid sequences of human and mouse Id-2 and Id-3 proteins, reveals conservation/divergence of several residues in the helix-loop-helix domain known to be important for heterodimerisation, together with a common casein kinase II phosphorylation site.

Amino Acid Sequence↗
PubMed1988

Nucleotide sequence analysis of cDNA encoding the coat protein of cucumber mosaic virus: genome organization and molecular features of the protein.

The cDNA sequence coding for the coat protein of cucumber mosaic virus (Japanese Y strain) was cloned, and its nucleotide sequence was determined. The sequence contains an open reading frame that encodes the coat protein composed of 218 amino acids. The nucleotide and deduced amino acid sequences of the coat protein of this strain were compared with those of the Q strain; the homologies of the sequences were 78% and 81%, respectively. Further study of the sequences gave an insight into the genome organization and the molecular features of the coat protein. The coding region can be divided into three characteristic regions. The N-terminal region has conserved features in the positively charged structure, the hydropathy pattern and the predicted secondary structure, although the amino acid sequence is varied mainly due to frameshift mutations. It is noteworthy that the positions of arginine residues in this region are highly conserved. Both the nucleotide and amino acid sequences of the central region are well conserved. The amino acid sequence of the C-terminal region is not conserved, because of frameshift mutations, however, the total number of amino acids is conserved. The nucleotide sequence of the 3'-noncoding region is divergent, but it could form a tRNA-like structure similar to those reported for other viruses. Detailed investigation suggests that the Y and Q strains are evolutionarily distant.

Amino Acid Sequence↗
PubMed1989

Cloning and sequence analysis of cDNA for luciferase of a Japanese firefly, Luciola cruciata.

Luciferases of Japanese and North American fireflies act on a common substrate (luciferin) but the resulting lights emitted are of different colors. As a step toward an understanding of the molecular mechanism of the luciferase reaction, a cDNA clone (pGLf1) was isolated from a cDNA library of lantern poly(A)+RNA of the Japanese firefly, Luciola cruciata ('Genji-botaru' in Japanese), using a cDNA of North American firefly luciferase. The isolated 2-kb cDNA sequence was able to direct the synthesis of active luciferase in Escherichia coli under the control of the lac promoter. The primary structure of Genji firefly luciferase deduced from the nucleotide sequence was shown to consist of 548 amino acids (aa) with an Mr of 60,024. Homology between the amino acid sequences of the Genji and North American firefly luciferases was 67%, but a number of amino acid changes were found in the first 200 aa from the N terminus.

Amino Acid Sequence↗
PubMed1995

Cloning and sequencing of a cDNA encoding a novel member of the human brain GABA/noradrenaline neurotransmitter transporter family.

Screening of a human hippocampal cDNA library with a rat creatine transporter cDNA-specific probe revealed two types of clones. One identical to the published creatine transporter cDNA sequence (CRT1) and another (CRT2) with four segments of oligodeoxyribonucleotide substitution or addition in different sites of the CRT1 coding sequence. Translation of the CRT2 coding sequence reveals a new protein with regions of perfect homology with the CRT1 amino-acid sequence.

Amino Acid Sequence↗
PubMed2004

Sequence analysis of cDNA encoding follicle-stimulating hormone and luteinizing hormone beta-subunits in the Mongolian gerbil (Meriones unguiculatus).

To examine the molecular basis for efficient superovulation in the Mongolian gerbil, the cDNA sequences of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) beta-subunits were determined and compared with those of other mammals. FSHbeta and LHbeta cDNAs were 1637 and 507bp long, respectively, from the 5'-end to putative polyA sites. The deduced sequences of the FSHbeta and LHbeta precursor proteins were 129 and 141 amino acids in length, respectively. The amino acid sequences of both Mongolian gerbil hormone subunits showed overall similarity to those of other rodents, confirming that the combination of equine chorionic gonadotropin (eCG) and human chorionic gonadotropin (hCG) should be effective for induction of superovulation in Mongolian gerbils, as in mice and rats. However, the use of hCG might need to be re-evaluated owing to its low homology to rodent LH.

Amino Acid Sequence↗
PubMed2004

Sequence analysis of cDNA encoding follicle-stimulating hormone and luteinizing hormone beta-subunits in the Mastomys (Praomys coucha).

To examine the molecular basis of efficient superovulation in the Mastomys (Praomys coucha), the cDNA sequences of the follicle-stimulating hormone (FSH) and luteinizing hormone (LH) beta-subunits were determined and compared with those of other mammals. FSHbeta and LHbeta cDNAs were 1606 and 513 bp long, respectively, from the 5'-ends to the putative polyA sites. The deduced sequences of the FSHbeta and LHbeta precursor proteins were 130 and 141 amino acids in length, respectively. The amino acid sequences of both mastomys hormone subunits showed overall similarity to those of other rodents. In particular, the N-terminus of the FSHbeta precursor protein is of the MM-type, like those of mice and rats, which suggests that the MM-type is characteristic of the subfamily Murinae. As we reported earlier for the Mongolian gerbil, the use of hCG for superovulation of mastomys might need to be re-evaluated, due to the low homology between hCG and rodent LH sequences.

Amino Acid Sequence↗
PubMed1998

Cloning and sequencing of the cDNA encoding human neurotrypsin.

cDNA clones encoding human neurotrypsin have been isolated from a human fetal brain cDNA library using a PCR-amplified probe. The assembled cDNA sequence contains a 2625 bp open reading frame encoding a multidomain serine protease with an overall sequence identity of 82.5% to murine neurotrypsin. Surprisingly, the human neurotrypsin exhibits an additional scavenger receptor cysteine-rich repeat.

Amino Acid Sequence↗
PubMed2003

Sequence of a cDNA encoding acetylcholinesterase from susceptible and resistant two-spotted spider mite, Tetranychus urticae.

Acetylcholinesterase (AChE) from two-spotted spider mites, Tetranychus urticae was compared between an organophosphate susceptible (TKD) and a resistant (NCN) strain. The AChE of TKD had lower affinity to acetylthiocholine and propionylthiocholine than that of NCN, and the inhibition of AChE by DDVP, ambenonium, eserine and n-methyl-eserine showed that NCN was more insensitive than TKD. AChE cDNA sequence was determined, and the 687 amino acids of primary structure were deduced. There were six replacements of amino acid residues in TKD and two in NCN. #F331(439)C was the only substitution unique to NCN, however, this mutation existed homozygously in only two out of nine mites. This residue is one of the gorge lining components, and #F331(439)C might act an important role in the sensitivity of AChE to the inhibitors.

Acetylcholinesterase↗
PubMed1993

cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase. Detection of a 3'-untranslated nucleotide sequence common to the mRNA of transiently expressed genes and rapid turnover of this enzyme's mRNA in the estrous cycle.

Peptidylarginine deiminase is a protein-modulating enzyme which converts the arginine residues in proteins to citrulline residues. This study describes the complete primary structure of mouse peptidylarginine deiminase, which was deduced from nucleotide sequence analysis of cDNA clones plus proteochemical analysis of the purified enzyme. The composite cDNA sequence contained a 5' untranslated region of 7 bases, an open reading frame of 2019 bases that encoded 673 amino acids, a 3' untranslated region of 2662 bases, and part of a poly(A) tail. The N-terminal and C-terminal sequences of the enzyme matched the sequences deduced from nucleotide analysis. Furthermore, we determined that the N-terminal sequence was N alpha-acetyl-Met-Gln-, a sequence which has never previously been reported among N alpha-acetyl-Met proteins. The Arg 352 of the enzyme was converted to a citrulline residue and the potential Asn-linked glycosylation site (Asn542-Glu543-Ser544) had no carbohydrate moiety. Thus, mouse peptidylarginine deiminase consists of 673 amino acids with a molecular mass of 76,260. Mouse peptidylarginine deiminase mRNA has two AU-rich structures in the 3' untranslated region which exhibit a high degree of similarity to those in lymphokine, cytokine and proto-oncogene mRNA species. Since the rat enzyme (previously reported) does not possess these characteristic structures, we compared the levels of enzyme activity and mRNA in the mouse and rat uterus at four defined phases of the estrous cycle. The degradation of peptidylarginine deiminase and its mRNA proceeded significantly faster in the mouse than in the rat. We speculate that the unusual structure of the mouse enzyme and its mRNA be involved in this species-specific rapid degradation.

Amino Acid Sequence↗
PubMed1989

Isolation and sequence of a cDNA clone of beta-nerve growth factor from the guinea pig prostate gland.

The guinea pig prostate gland contains high levels of nerve growth factor similarly to the mouse submandibular gland. Nerve growth factor from the guinea pig prostate gland cross-reacts weakly with antisera directed against mouse nerve growth factor, is associated with different proteins, and may be processed by a different mechanism. We have isolated a full-length cDNA clone for nerve growth factor from a library prepared from RNA of the guinea pig prostate gland. The guinea pig cDNA contains 1,075 nucleotides and is very similar to the shorter of two predominant nerve growth factor transcripts present in the mouse submandibular gland. The cDNA sequence predicts a precursor protein of 241 amino acids that is 86% identical to the mouse amino acid sequence. Only 10 amino acid changes are present in the C-terminal region corresponding to the mature 118 amino acid beta-nerve growth factor of the mouse. Dibasic amino acid processing sites that are present at the N- and C-termini of the mature protein sequence and two other dibasic amino acid sites, representing potential processing sites within the propeptide, are all conserved, suggesting a similar mechanism of processing.

Amino Acid Sequence↗
PubMed1985

Cloning and sequence analysis of a cDNA encoding porcine mitochondrial aspartate aminotransferase precursor.

The primary structure of pig mitochondrial aspartate aminotransferase (mAspATase; L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) precursor was deduced from its cDNA sequence. A library of cDNA clones was constructed from pig liver poly(A)+ RNA by applying the vector/primer method of Okayama and Berg [Okayama, H. & Berg, P. (1982) Mol. Cell. Biol. 2, 161-170]. The library was screened for pig mAspATase sequences by using a mixture of eight oligodeoxyribonucleotides as a probe. The sequences of the probe were deduced from the known amino acid sequence of pig mAspATase residues 196-201. Two recombinant plasmids containing inserts of about 2500 and 2600 base pairs were selected for sequence analysis. The amino acid sequence predicted from the cDNA sequence shows that the pig mAspATase precursor consists of the mature enzyme of 401 amino acid residues and an amino-terminal segment of 29 amino acid residues called the "presequence" that contains four basic amino acid residues, no acidic residues, and no hydrophobic amino acid stretch. The sequence of this 29-amino acid mAspATase precursor segment was compared with the presequences of other mitochondrial enzymes.

Amino Acid Sequence↗
PubMed1989

cDNA cloning and sequence and cDNA-directed expression of human P450 IIB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver.

A cDNA designated hIIB1, representing the entire coding sequence of a P450 in the IIB gene family, was isolated from a human liver lambda gt11 library by using the rat IIB1 cDNA as a probe. The hIIB1 protein, deduced from the cDNA sequence, contained 491 amino acids, had a calculated molecular weight of 56,286, and displayed 76% amino acid similarity with the rat IIB1 protein. Expression of this cDNA, using the vaccinia virus system, yielded a P450 that had a reduced CO-binding spectrum with an absorption maximum of 452 nm. The expressed human enzyme was able to catalyze the deethylation of 7-ethoxy-coumarin. Total RNA from 13 livers was probed for levels of hIIB mRNA. Two livers had high levels, four contained moderate levels, and eight contained very low, or no detectable, mRNA. These data suggest either that defective hIIB1 genes exist in humans or that the hIIB1 gene is regulated and variably induced in our liver specimens. To search for mutant mRNA transcripts, libraries were constructed from livers expressing low levels of hIIB1 mRNA. A cDNA, designated hIIB2, was isolated that was identical with the hIIB1 cDNA except for the presence of an unusual alteration of the DNA near its 5' end corresponding to the putative exon 4. This alteration was caused by a deletion of 29 bp and an insertion of 44 bp of nonhomologous DNA. This sequence replacement occurs at the junction of the third and fourth exons as predicted from the structure of the rat IIB1 gene, suggesting that a faulty splice might have given rise to the variant hIIb2 transcript.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗