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Query: UNIPROT:P06889 (Mol)
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We have previously shown that the expression of pS2 mRNA, which encodes a secreted 60-amino acid protein of unknown function, is widely distributed throughout the entire body of the mouse including the brain. We report herein that pS2 mRNA is also expressed in the brain and in peripheral tissues of rats. In adult rat brain, pS2 mRNA was predominantly expressed in hippocampus, followed by the cerebral cortex and cerebellum. The developmental expression of pS2 mRNA in hippocampus, which region is known to mature after birth, showed a clear peak in 1- or 3-day-old rats, then gradually decreased by 7 weeks after birth. In midbrain, the maturation of which occurs at an early developmental stage, pS2 mRNA level was retained at a low level from postnatal 1 day to week 7. These results suggest that pS2 protein plays an important role in the development of central nervous system.
Biochem Mol Biol Int 1995 Apr
PMID:Expression of pS2 gene in rat brain. 754 26

The toxin coregulated pilus (TCP) is required for Vibrio cholerae to colonize the human intestine. The expression of the pilin gene, tcpA, is dependent upon ToxR and upon ToxT. The toxT gene was recently mapped within the TCP biogenesis gene cluster and shown to be capable of activating a tcpA::TnphoA fusion when cloned in Escherichia coli. In this study, we determined that ToxR/ToxT activation occurs at the level of tcpA transcription. ToxT expressed in E. coli could activate a tcp operon fusion, while ToxR, ToxR with ToxS, or a ToxR-PhoA fusion failed to activate the tcp operon fusion and we could not demonstrate binding of a ToxR extract to the tcpA promoter region in DNA mobility-shift assays. The start site for the regulated promoter was shown by primer extension to lie 75 bp upstream of the first codon of tcpA. An 800-base tcpA message was identified, by Northern analysis, that correlates by size to the distance between the transcriptional start and a hairpin-loop sequence between tcpA and tcpB. The more-sensitive assay of RNase protection analysis demonstrated that a regulated transcript probably extends through the rest of the downstream tcp genes, including toxT and the adjacent accessory colonization factor (acf) genes. An in-frame tcpA deletion, but not a polar tcpA::TnphoA fusion, could be complemented for pilus surface expression by providing tcpA in trans. This evidence suggests that the tcp genes, including toxT, are organized in an operon directly activated by ToxT in a ToxR-dependent manner. Most of the toxT expression under induced conditions requires transcription of the tcpA promoter. Further investigation of how tcp::TnphoA insertions that are polar on toxT expression retain regulation showed that a low basal level of toxT expression is present in toxR and tcp::TnphoA strains. Overall, these observations support the ToxR/ToxT cascade of regulation for tcp. Once induced, toxT expression becomes autoregulatory via the tcp promoter, linking tcp expression to that of additional colonization factors, exotoxin production, and genes of unknown function in cholera pathogenesis.
Mol Microbiol 1995 May
PMID:Organization of tcp, acf, and toxT genes within a ToxT-dependent operon. 756 4

osmE, an osmotically inducible gene of Escherichia coli, was physically mapped on the bacterial chromosome, cloned and sequenced. osmE appeared to encode a 12,021 Da protein of unknown function, with a lipoprotein-type signal sequence at the amino-terminus. The osmE reading frame was confirmed by sequencing the junction of an osmE-phoA gene fusion. osmE was demonstrated to be transcribed as a single cistron. A phi [osmEp-lac] operon fusion was constructed, and analysis of its expression demonstrated that osmE osmotic regulation probably occurs at the transcriptional level. The osmE promoter was identified by both S1 nuclease and primer extension mapping of the 5' end of the osmE mRNA, by deletion analysis and by identification of a point mutation reducing its activity. Sequence information sufficient for expression and osmotic regulation is present on a DNA fragment extending from positions -37 to +52 with respect to the osmE transcription start. Uninduced expression of the osmE-lac fusion was increased in the presence of mutations in the hns and himA genes. The osmE promoter overlaps a promoter for a gene transcribed in the opposite direction, efg. Transcription from the efg promoter is only weakly affected by osmotic pressure and is independent of the presence of an intact OsmE protein.
Mol Microbiol 1995 May
PMID:Characterization of the osmotically inducible gene osmE of Escherichia coli K-12. 756 14

We identified and isolated a Saccharomyces cerevisiae gene which, when overexpressed, suppressed the temperature-sensitive phenotype of cells expressing a mutant allele of the gene encoding the mitochondrial chaperonin, Hsp60. This gene, SCS1 (suppressor of chaperonin sixty-1), encodes a 757-amino-acid protein of as yet unknown function which, nonetheless, has human, rice, and Caenorhabditis elegans homologs with high degrees (ca. 60%) of amino acid sequence identity. SCS1 is not an essential gene, but SCS1-null strains do not grow above 37 degrees C and show some growth-related defects at 30 degrees C as well. This gene is expressed at both 30 and 38 degrees C, producing little or no differences in mRNA levels at these two temperatures. Overexpression of SCS1 could not complement an HSP60-null allele, indicating that suppression was not due to the bypassing of Hsp60 activity. Of 10 other hsp60-ts alleles tested, five could also be suppressed by SCS1 overexpression. There were no common mutant phenotypes of the strains expressing these alleles that give any clue as to why they were suppressible while others were not. An epitope (influenza virus hemagglutinin)-tagged form of SCS1 in single copy complemented an SCS1-null allele. The Scs1-hemagglutinin protein was found to be at comparable levels and in similar multiply modified forms in cells growing at both 30 and 38 degrees C. Surprisingly, when localized either by cell fractionation procedures or by immunocytochemistry, these proteins were found not in mitochondria but in the cytosol. The overexpression of SCS1 had significant effects on the cellular levels of mRNAs encoding the proteins Cpn10 and Mgel, two other mitochondrial protein cochaperones, but not on mRNAs encoding a number of other mitochondrial or cytosolic proteins analyzed. The implications of these findings are discussed.
Mol Cell Biol 1995 Oct
PMID:SCS1, a multicopy suppressor of hsp60-ts mutant alleles, does not encode a mitochondrially targeted protein. 756 13

Elongation factors G, Tu, and related proteins (including LepA) form a distinct subgroup within the GTPase superfamily. This observation is based primarily upon amino acid comparisons of the effector region (G2) of the GTP-binding domain. To examine the functional importance of the highly conserved elongation factor G2 domain a series of chimeric proteins were constructed between Escherichia coli EF-G and Micrococcus luteus EF-G, and between E. coli EF-G and LepA (a protein of unknown function). The M. luteus EF-G/E. coli EF-G hybrid, M. luteus EF-G, and E. coli EF-G efficiently complemented EF-G function in an E. coli strain (PEM101) harbouring a temperature-sensitive mutation in fusA (the gene encoding EF-G). A comparison of the amino acid sequences of the M. luteus EF-G and E. coli EF-G indicated that groups of divergent amino acid residues (amino acids 1-9 and 72-80) were not important for function. LepA and LepA/EF-G chimeric proteins were tested for the ability to complement EF-G function in vivo, for cross-linking to 8-azido-[gamma-32P]-GTP in vitro and for fusidic acid-dependent co-sedimentation with 70S ribosomes. With one exception, all chimeras could be readily cross-linked to azido-GTP in an EF-G-like manner, indicating that hybrid protein construction did not generally result in improperly folded GTP-binding domains. However, the inability of such chimeras to complement EF-G function in vivo indicates that the effector domains are not functionally interchangeable. All LepA/EF-G chimeric proteins were severely defective in fusidic acid-dependent complex formation with 70S ribosomes. A comparison of the amino acid sequences of all three proteins suggests that residues 30-33, 43-48, and 63-66 of E. coli EF-G are important for EF-G specific ribosome-associated function.
Mol Microbiol 1995 Mar
PMID:Small clusters of divergent amino acids surrounding the effector domain mediate the varied phenotypes of EF-G and LepA expression. 759 95

In the present study, we have constructed a subtraction cDNA library to identify novel genes induced by IFN-gamma in GM-CSF-derived bone marrow macrophage (m phi). M theta were treated with 50 U/ml IFN-gamma for 40, 70 and 140 min to induce expression of early genes regulated by IFN-gamma, and the M phi were pooled. Poly(A)+RNA was prepared from both unactivated and IFN-gamma-stimulated m theta, and cDNA libraries were constructed in lambda ZAP. Genes expressed in common by both m theta populations were removed by subtraction using biotin-avidin precipitation of hybrid complexes. Further selection was performed by differential screening using cDNA prepared from mRNA of unactivated m phi as a probe, followed by colony hybridization to remove sister clones. Of 17 clones from which sequence information was obtained, two appeared to be identical with the murine genes, C10 (clone GM2B1) and Mac-2 (clone GM2C4) and an additional two clones had high similarity to human cDNAs encoding proteins of unknown function. cDNAs containing sequences which did not match published sequences were used to probe Northern blots prepared from both unstimulated and IFN-gamma-activated GM-CSF- and CSF-1-derived m phi. Five clones (GM1A2, GM1B4, GM1F2, GM2A12 and GM2B8) showed enhanced transcript levels following IFN-gamma treatment of GM-CSF-derived m phi, but demonstrated high constitutive transcript levels in CSF-l-derived m phi. In addition, C10 transcripts were constitutively expressed by GM-CSF-derived m phi, but not by CSF-1-derived m phi, even after activation by IFN-gamma. These data suggest that much of the functional heterogeneity of GM-CSF- and CSF-1-derived m phi resides in the differential expression of early genes specifically induced by IFN-gamma.
Mol Immunol 1995 Jul
PMID:Differential expression of novel genes by bone marrow-derived macrophage populations. 765 99

Drosophila adipokinetic hormone (DAKH) is an eight amino acid member of a large arthropod neuropeptide family. The gene encoding the peptide precursor has been identified and sequenced providing an inferred precursor structure of 79 amino acids including a 46 amino acid carboxy-terminal fragment of unknown function. In situ hybridization identifies sites of DAKH synthesis towards the base of the third larval instar ring gland. Like other RPCH (red pigment concentrating hormone)/AKH family peptides, DAKH can act as a cardioaccelerator at least in prepupae. Peptide levels measured in wildtype and mutant flies possessing one or three copies of the DAKH gene suggest that the amount of neuropeptide per fly is tightly regulated.
Mol Cell Endocrinol 1995 Apr 01
PMID:Identification and expression of the Drosophila adipokinetic hormone gene. 766 75

B1 and Alu are sequence-homologous interspersed elements of unknown function that have expanded in the genomes of mice and humans, respectively. A minority of B1 and Alu sequences are expressed as small cytoplasmic RNAs. These RNAs have conserved a secondary structure motif also present in signal recognition particle (SRP) RNA despite substantial sequence divergence, whereas random B1 and Alu sequences have not. This RNA structure has also been conserved by the source sequences that gave rise to successive transpositions during B1 and Alu evolution. In the present work small cytoplasmic B1 and Alu RNAs synthesized in vitro were found to bind a cellular protein by mobility shift and UV cross-linking analyses. The mouse and human proteins demonstrate the same specificity to a panel of competitor RNAs. Results using mutated B1 RNA indicate that a single strand loop in the conserved Alu motif is essential for binding. Previous work by Strub et al. (Stub, K., Moss, J. B., and Walter, P. (1991) Mol. Cell. Biol. 11, 3949-3959) demonstrated that the Alu-specific protein SRP 9/14 does not footprint to this region of SRP RNA. This observation coupled with the failure of anti-SRP/9 antibodies to identify SRP 9/14 in the B1 RNA-protein complex as well as the apparent mass and other characteristics of the protein described here suggest that it is a novel B1-Alu RNA-binding protein. Conservation of primary and secondary structure by B1 and Alu small cytoplasmic RNAs as well as features of their specific expression and ability to interact with the conserved binding protein indicate that these RNAs are more homologous than previously appreciated.
 ...
PMID:A cellular protein binds B1 and Alu small cytoplasmic RNAs in vitro. 768 Oct 65

In the rat, injection of Freund's complete adjuvant was accompanied by a significant increase in concanavalin A (Con A)-reactivity of selected plasma proteins along with an increase in concentrations of selected proteins known as acute phase proteins. We have evaluated the effect of bindarit, (2-[(1-benzyl-indazol-3-yl)methoxy]-2-methyl propionic acid), on the expression of alpha 2-macroglobulin, a known acute-phase protein in the rat. This compound has previously been shown to inhibit heat-induced denaturation of rat serum albumin and to strongly reduce the secondary phase response of adjuvant induced arthritis. Adult rats were induced with chronic inflammation by injection with Freund's complete adjuvant. Bindarit was administered to the chronic inflamed rats as a 0.5% medicated diet. Indomethacin, given by gavage daily at a dose of 1 mg/kg body weight, was used as a reference drug. Qualitative and quantitative changes of Con A-reactive proteins and alpha 2-macroglobulin were examined by lectin- and immuno-blots, and by radioimmunoassay. It was noted that the concentration of alpha 2-macroglobulin increased in rats with adjuvant induced arthritis. The addition of bindarit and indomethacin were able to reduce the concentration of alpha 2-macroglobulin as well as the Con A-reactivity of various proteins to normal level 37 days following treatment. We have also examined the effects of chronic inflammation on the levels of rat clusterin, a testicular and serum glycoprotein related to programmed cell death, tissue regression, and complement cascade reaction; and testibumin, a testicular FSH and testosterone-responsive protein with unknown function. It was noted that chronic inflammation did not induce significant changes in both the clusterin and testibumin concentrations in these experimental groups. The involvement of protein glycosylation and denaturation in the production of new antigenic determinants, their role in the development of chronic inflammatory disease and the potential use of bindarit to investigate the relationship between abnormal glycosylation and autoimmune disease were discussed.
Biochem Mol Biol Int 1993 Mar
PMID:Chronic inflammatory response in the rat can be blocked by bindarit. 768 47

Kidney androgen-regulated protein (KAP) is a unique protein of unknown function that is transcriptionally induced by sex steroids. KAP is thought to be predominantly a kidney-specific gene. After conducting a differential screen of a mouse uterus cDNA library, a clone was identified that is identical to KAP. Using this cDNA to generate radiolabeled cRNA probes, Northern blots were conducted against the following tissues collected sequentially during the latter third of pregnancy: kidney, uterus and placenta. Abundant message was present in all samples of the kidney tested and there was a slight, but apparent, increase (1.5-fold) in expression during the period surrounding birth. Message is also present in the uterus, at levels comparable to the kidney, but expression occurs only during the period surrounding birth. Message is not present in the uterus at any other time. Message is also not detected in the placenta or in several other tissues tested. In addition to the kidney, KAP gene is also transcribed at equivalent levels in the uterus. Unlike the kidney, expression in the uterus is limited to the perinatal period.
Mol Cell Endocrinol 1993 Jan
PMID:Kidney androgen-regulated protein gene is expressed in the uterus during late pregnancy. 768 43


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