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PubMed1993

Molecular cloning of cDNA encoding the phenol/aryl form of sulfotransferase (mSTp1) from mouse liver.

The cDNA sequence of the mouse liver phenol/aryl form of sulfotransferase (mSTp1) has been determined. The cloned cDNA consists of 1269 base pairs (bp) and contains an 897 nucleotide open reading frame (ORF) beginning at nucleotide 65, which encodes a 298 amino acid polypeptide of 34.7 kDa. Alignment of mSTp1 to other sulfotransferases shows overall identities of 87% to r-STp, 37% to r-STa, 48% to r-STe, 51% to b-STe, and 37% to h-STa, at the deduced amino acid level.

Amino Acid Sequence↗

PubMed1994

Structure and analysis of the 5' flanking region of the human interleukin-2 gene.

To investigate the structural and functional organization of the human interleukin-2 locus, the nucleotide sequence of 9339 bp of the 5' flanking region of this gene has been determined. Computer search analysis reveals five stretches with a high degree of homology between the human and mouse 5' flanking sequence, including a very distant 5' region. In this region additional binding sites for potential transcription factors were found that are identical to known regulatory sequences. The possible roles of these putative regulatory elements in the interleukin-2 gene regulation remain to be proven. The 5' end of the sequence contains almost full-length LINE element. LINE consensus open reading frames ORF1 and ORF2 in the reported sequence are interrupted by insertions, deletions or in-frame nonsense mutations. Comparative analysis of the ratio of codon changes that result in amino acid replacement to those that are silent revealed a high silent mutation frequency throughout the consensus ORF1 3' end, suggesting that this region is probably under selection for protein function.

Amino Acid Sequence↗

PubMed2000

Evidence for the existence of rhodanese (thiosulfate:cyanide sulfurtransferase) in plants: preliminary characterization of two rhodanese cDNAs from Arabidopsis thaliana.

The existence of rhodanese (thiosulfate:cyanide sulfurtransferase; EC 2.8.1.1) in plants has been highly controversial. We have isolated and characterized for the first time in plants two cDNAs encoding rhodanese isoforms in Arabidopsis thaliana, AtRDH1 and AtRDH2. Both cDNAs contained a full-length open reading frame, the expression of which increased the rhodanese activity of transgenic yeast. AtRDH1 protein was mitochondrial, while AtRDH2 was cytosolic. AtRDH1 and AtRDH2 genes originated from the duplication of a large genomic region in chromosome 1 which took place before the appearance of the Arabidopsis genus. Our results confirm the existence of rhodanese in plants.

Amino Acid Sequence↗

PubMed1998

Sequence and expression in Escherichia coli of the coat protein gene of the dwarfing strain of soybean dwarf luteovirus.

The nucleotide sequence of the coat protein gene of the dwarfing (D) strain of soybean dwarf luteovirus (SbDV) was determined from cloned cDNA. The gene contains 600 nucleotides and encodes a protein of 200 amino acids with a calculated molecular mass of 22.2 kDa. A major portion of the coat protein open reading frame (ORF) was expressed in Escherichia coli as a pET fusion protein and the product was detected by western blot analysis using SbDV-D polyclonal antibodies. Comparison of the deduced coat protein amino acid sequence to that from the yellowing (Y) strain of SbDV demonstrated 88% identity.

Amino Acid Sequence↗

PubMed1997

Generation of cDNA expression libraries enriched for in-frame sequences.

Bacterial cDNA expression libraries are made to reproduce protein sequences present in the mRNA source tissue. However, there is no control over which frame of the cDNA is translated, because translation of the cDNA must be initiated on vector sequence. In a library of nondirectionally cloned cDNAs, only some 8% of the protein sequences produced are expected to be correct. Directional cloning can increase this by a factor of two, but it does not solve the frame problem. We have therefore developed and tested a library construction methodology using a novel vector, pKE-1, with which translation in the correct reading frame confers kanamycin resistance on the host. Following kanamycin selection, the cDNA libraries contained 60-80% open, in-frame clones. These, compared with unselected libraries, showed a 10-fold increase in the number of matches between the cDNA-encoded proteins made by the bacteria and database protein sequences. cDNA sequencing programs will benefit from the enrichment for correct coding sequences, and screening methods requiring protein expression will benefit from the enrichment for authentic translation products.

Base Sequence↗

PubMed1991

A molecular analysis of the 53.3 minute region of the Escherichia coli linkage map.

The coding characteristics of four plasmids expressing a protein (BCP) which comigrates with bacterioferritin were examined and the nucleotide sequence of a common 1985 bp segment from the 53 min region of the Escherichia coli linkage map was determined. Three open reading-frames (orf1, orf2 and orf3) were detected, and orf2 (bcp, 156 amino acid codons) appeared to encode the bacterioferritin comigratory protein, BCP. The translation product of orf3 (205 amino acid codons) resembled the iron-sulphur protein component (DMS B subunit) of the anaerobic dimethylsulphoxide reductase complex of E. coli.

Amino Acid Sequence↗

PubMed1995

Product of fosC, a gene from Pseudomonas syringae, mediates fosfomycin resistance by using ATP as cosubstrate.

Pseudomonas syringe PB-5123, a producer of fosfomycin, is resistant to high concentrations of the antibiotic. Two possible mechanisms of resistance have been detected: (i) impermeability to exogenous fosfomycin, even in the presence of sugar phosphate uptake inducers, and (ii) antibiotic phosphorylation. The gene responsible for this last activity, fosC, encodes a ca. 19,000-Da protein and is immediately followed by a second open reading frame, which shows sequence similarities to glutathione S-transferases. FosC uses ATP as a cosubstrate in an inactivation reaction that can be reversed with alkaline phosphatase. Other nucleotide triphosphates cannot be substituted for ATP in this reaction. No relationship between fosC and the previously described genes of fosfomycin resistance was found.

Adenosine Triphosphate↗

PubMed1999

Identification of an efflux pump gene, pmrA, associated with fluoroquinolone resistance in Streptococcus pneumoniae.

An open reading frame (ORF) homologous to norA was insertionally inactivated with cat in a fluoroquinolone-resistant pneumococcus with an efflux phenotype; this inactivation caused reversion to drug sensitivity. The ORF product has 24% amino acid sequence identity each to NorA and Bmr, which suggests that it is a major facilitator system pump of the 12-transmembrane-segment class.

Amino Acid Sequence↗

PubMed1996

A moderately repetitive DNA sequence in alfalfa is transcribed in a floral-specific manner.

Based on DNA sequence analysis of 5 clones of repetitive DNA from alfalfa (Medicago sativa), we propose the existence of a dispersed middle repetitive element about 3400 bp long with a copy number in the range of 2-3 x 10(3) per haploid genome. The average A+T content of the sequences was 54.6%, compared with 61.4% for the alfalfa genome. Sequence homologies between overlapping regions of the clones ranged from 85 to 89.5% with an average of 86.6%; sequence divergence was due largely to single base pair changes, with deletions or insertions occurring randomly across sequences. An open reading frame (ORF) in one clone, RPE15, contained homologies to cereal prolamin genes and a legumin box was located upstream of the coding region. A Northern blot of RNA from various alfalfa tissues, probed with the above clone containing this ORF, showed an extensive heterodispersed pattern of hybridization in the late stages of flower bud development but in no other tissues.

Base Composition↗

PubMed1993

Sequence analysis of the lysin gene region of the prolate lactococcal bacteriophage c2.

Approximately 80% of the genome of the prolate-headed lactococcal bacteriophage c2 was cloned into shuttle vectors pSA3 and pFX3 in Escherichia coli and transferred to Lactococcus lactis. A 1.67-kilobase EcoRV fragment containing the gene for the phage lysin was identified and the position and orientation of the phage lysin gene in the physical map of the phage were determined. The phage lysin was expressed in E. coli and its sequence was determined and compared with the sequences of other bacteriophage lytic genes. The sequence was similar, but not identical, to that of the related lactococcal phage m13, having a number of silent substitutions and an apparent deletion that altered the carboxy terminus of the protein. Possible alternative translation initiation codons for the lysin gene and two possible alternative mechanisms for access of the lysin enzyme to the cell wall are discussed. An open reading frame upstream of the putative lysin gene was found to be 177 base pairs longer than that reported for phage m13. A codon usage table for the lysin genes of several phages as well as for reported gene sequences from L. lactis and lactococcal bacteriophages is presented.

Amino Acid Sequence↗

PubMed1999

Assignment of Pdnp2, the gene encoding phosphodiesterase I/nucleotide pyrophosphatase 2, to mouse chromosome 15D2.

We have isolated cDNA and genomic DNA encoding mouse PDNP2 (PD-Ialpha). The mouse Pdnp2 cDNA contains a 2,589-nucleotide open reading frame encoding a polypeptide of 863 amino acids. The 5' region of the mouse Pdnp2 gene contains Sp1, Max1, HNF-3B, and AP1 putative transcription factor binding sites, without typical TATA or CAAT boxes. Fluorescence in situ hybridization showed that Pdnp2 is located at Chromosome 15D2, as expected based on mouse-human conserved regions.

Animals↗

PubMed1992

Analysis of bph operon from the polychlorinated biphenyl-degrading strain of Pseudomonas pseudoalcaligenes KF707.

The entire nucleotide sequences (6.8 kilobase pairs) of the bphABC genes and their products involved in the initial dioxygenation and ring-meta-cleavage of biphenyls and polychlorinated biphenyls were determined. The first bphA gene starts about a 100 base pairs downstream from the transcriptional initiation site. The bphA region, which encodes a cluster of enzymes including biphenyl dioxygenase catalyzing the initial catabolic step, consists of five open reading frames (ORFs). Five proteins corresponding to these ORFs in the molecular masses were detected by in vitro protein synthesis, of which four ORFs are very similar to the recently reported todC1C2BA genes coding for the corresponding enzymes catalyzing the initial dioxygenation reactions of toluene (Zylstra, G.J., and Gibson, D. T. (1989) J. Biol. Chem. 264, 14940-14946). The third open reading frame (ORF3) of the bphA region, missing its counterpart in the toluene dioxygenase gene cluster, was site-specifically deleted, and the resulting enzymatically active mutant reveals that this ORF3 is not mandatory for the catabolism of biphenyls. Thus the biphenyl degradation pathway and the responsible enzymes/genes are very similar to those of toluene degradation despite their discrete substrate specificity.

Amino Acid Sequence↗

PubMed1990

[Features of the structural organization of the MDG1 retrotransposon of Drosophila, revealed during its sequencing].

The two long open reading frames (ORF1 and ORF2) have been identified in the primary structure of the full-length copy of mdg1 Drosophila retrotransposon by the sequence analysis. These two partially overlapping frames code for the necessary information for transposition through the reverse transcription mechanism. There are unusually long leader and terminal regions in mdg1. The leader area contains two small open reading frames. One of them includes the information of a polypeptide with the typical zinc-binding region. Long oligo (dA) sequences separate the small ORFs from each other and from the long ORFs. Considerable homology between the MDG1 and 412 mobile elements has been detected by comparative analysis of their sequences. The common ancestor of these two elements is postulated.

Amino Acid Sequence↗

PubMed2004

The 1.2-megabase genome sequence of Mimivirus.

We recently reported the discovery and preliminary characterization of Mimivirus, the largest known virus, with a 400-nanometer particle size comparable to mycoplasma. Mimivirus is a double-stranded DNA virus growing in amoebae. We now present its 1,181,404-base pair genome sequence, consisting of 1262 putative open reading frames, 10% of which exhibit a similarity to proteins of known functions. In addition to exceptional genome size, Mimivirus exhibits many features that distinguish it from other nucleocytoplasmic large DNA viruses. The most unexpected is the presence of numerous genes encoding central protein-translation components, including four amino-acyl transfer RNA synthetases, peptide release factor 1, translation elongation factor EF-TU, and translation initiation factor 1. The genome also exhibits six tRNAs. Other notable features include the presence of both type I and type II topoisomerases, components of all DNA repair pathways, many polysaccharide synthesis enzymes, and one intein-containing gene. The size and complexity of the Mimivirus genome challenge the established frontier between viruses and parasitic cellular organisms. This new sequence data might help shed a new light on the origin of DNA viruses and their role in the early evolution of eukaryotes.

Acanthamoeba↗

PubMed2006

Identification and characterization of the Orf49 protein of Kaposi's sarcoma-associated herpesvirus.

Kaposi's sarcoma-associated herpesvirus (KSHV) is the etiological agent of Kaposi's sarcoma, primary effusion lymphoma, and multicentric Castleman's disease. Kaposi's sarcoma is the most common neoplasm among human immunodeficiency virus-positive individuals. Like other herpesviruses, KSHV is able to establish a predominantly latent, life-long infection in its host. The KSHV lytic cycle can be triggered by a number of stimuli that induce the expression of the key lytic switch protein, the replication and transcription activator (RTA) encoded by Orf50. The expression of Rta is necessary and sufficient to trigger the full lytic program resulting in the ordered expression of viral proteins, release of viral progeny, and host cell death. We have characterized an unknown open reading frame, Orf49, which lies adjacent and in the opposite orientation to Orf50. Orf49 is expressed during the KSHV lytic cycle and shows early transcription kinetics. We have mapped the 5' and 3' ends of the unspliced Orf49 transcript, which encodes a 30-kDa protein that is localized to both the nucleus and the cytoplasm. Interestingly, we found that Orf49 was able to cooperate with Rta to activate several KSHV lytic promoters containing AP-1 sites. The Orf49-encoded protein was also able to induce transcriptional activation through c-Jun but not the ATF1, ATF2, or CREB transcription factor. We found that Orf49 could induce phosphorylation and activation of the transcription factor c-Jun, the Jun N-terminal kinase (JNK), and p38. Our data suggest that Orf49 functions to activate the JNK and p38 pathways during the KSHV lytic cycle.

Animals↗

PubMed1995

The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII reveals the presence of eight open reading frames.

The complete sequence of a 11, 132 bp segment located on the left arm of chromosome VII of Saccharomyces cerevisiae has been determined and analysed. Eight open reading frames (ORFs) of at least 100 amino acids were identified. Five show similarities to known amino acid sequences. Another ORF encoding the chromosome segregation protein CSE1 is not entirely located in our sequenced fragment and is incomplete at its C-terminus. The two remaining ORFs do not display similarities to known sequences.

Adenosine Deaminase↗

PubMed2001

Lupus autoantibodies recognize the product of an alternative open reading frame of SmB/B'.

An unusual feature of the gene for the spliceosomal protein SmB/B' is the presence of an unusually long alternative open reading frame (aORF) which could encode 220 amino acids. We cloned and expressed this aORF protein and used immunological assays to determine its antigenicity in patients with systemic lupus. Sera from 10 of 22 (46%) anti-Sm positive lupus patients showed significant binding to the SmB' aORF protein by ELISA while neither the normal controls nor anti-Sm negative lupus patient controls showed significant reactivity. Antigenicity of the SmB' aORF protein was further localized to the C-terminus using a deletion construct. This is the first known example in which the product of an alternative open reading frame acts as an autoantigen in human disease. These results are consistent with the possibility that generation of anti-Sm autoantibodies in a subset of lupus patients is due to abnormal processing and expression of an aORF SmB/B' message, by an as yet unidentified mechanism.

Adult↗

PubMed1993

Identification of the purA gene encoding adenylosuccinate synthetase in Thiobacillus ferrooxidans.

The purA gene of Thiobacillus ferrooxidans encoding adenylosuccinate synthetase [EC 6.3.4.4] was identified in the upstream region of the iro gene encoding Fe(II)-oxidase (J. Biol. Chem 267:11242-11247, 1992). The purA gene consisted of 1290 base-pairs, which translated into a 29-amino-acid protein. The gene is functionally active, because it is able to complement an Escherichia coli purA-deficient strain. The deduced gene product has a high degree (60.9%) of sequence identity with that (432 aa) of E. coli purA gene, and both the products share GDEGKGK-DETG-TKLD sequences which are supposed to be GTP-binding domain. The downstream region of the iro gene contained another open-reading frame (ORF) of 1218 bp, and this showed high homology (56.6% over 249 bp) with E. coli ORF-II, which is found as a second ORF and truncated form in the downstream region of the purA gene. Comparison of the gene organization in the flanking region of purA gene between T. ferrooxidans and E. coli is also described.

Adenylosuccinate Synthase↗