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At least 37 records · Page 2Linked to original sources

PubMed2002

Episodic action memory for real objects: an ERP investigation with perform, watch, and imagine action encoding tasks versus a non-action encoding task.

Cognitive research shows that people typically remember actions they perform better than those that they only watch or imagine doing, but also at times misremember doing actions they merely imagined or planned to do (source memory errors). Neural research suggests some overlap between brain regions engaged during action production, motor imagery, and action observation. The present study evaluates the similarities/differences in brain activity during the retrieval of various types of action and nonaction memories. Participants study real objects in one of four encoding conditions: performing an action, watching the experimenter perform an action, or imagining an action with an object, or a nonmotoric task of estimating an object's cost. At test, participants view color photos of the objects, and make source memory judgments about the initial encoding episodes. Event-related potentials (ERPs) during test reveal (1) content-specific brain activity depending on the nature of the encoding task, and (2) a hand tag, i.e., sensitivity to the hand with which an object had been manipulated at study. At fronto-central sites, ERPs are similar for the three action-retrieval conditions, which are distinct from those to the cost-encoded objects. At occipital sites ERPs distinguished objects from encoding conditions with visual motion (Perform and Watch) from those without visual motion (Imagine and Cost). Results thus suggest some degree of recapitulation of encoding brain activity during retrieval of memories with qualitatively distinct attributes.

Adolescent↗

PubMed1999

Genes encoding three new members of the leukocyte antigen 6 superfamily and a novel member of Ig superfamily, together with genes encoding the regulatory nuclear chloride ion channel protein (hRNCC) and an N omega-N omega-dimethylarginine dimethylaminohydrolase homologue, are found in a 30-kb segment of the MHC class III region.

Many of the genes in the class III region of the human MHC encode proteins involved in the immune and inflammatory responses. We have sequenced a 30-kb segment of the MHC class III region lying between the heat shock protein 70 and TNF genes as part of a program aimed at identifying genes that could be involved in autoimmune disease susceptibility. The sequence analysis has revealed the localization of seven genes, whose precise position and order is cen-G7-G6-G6A-G6B-G6C-G6D-G6E-tel, five of which are fully encoded in the sequence, allowing their genomic structures to be defined. Three of them (G6C, G6D, and G6E) encode putative proteins that belong to the Ly-6 superfamily, known to be GPI-anchored proteins attached to the cell surface. Members of the family are specifically expressed and are important in leukocyte maturation. A fourth gene, G6B, encodes a novel member of the Ig superfamily containing a single Ig V-like domain and a cytoplasmic tail with several signal transduction features. The G6 gene encodes a regulatory nuclear chloride ion channel protein, while the G6A gene encodes a putative homologue of the enzyme N omega,N omega-dimethylarginine dimethylaminohydrolase, which is thought to be involved in regulating nitric oxide synthesis. In addition, three microsatellite markers, 9N-1, 82-2, and D6S273 are contained within the sequence, the last two of which have been reported to be strongly associated with the autoimmune disease ankylosing spondylitis.

Amidohydrolases↗

PubMed1988

Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein.

The c-erbA proto-oncogene encodes a nuclear receptor for thyroid hormone (T3), which is believed to stimulate transcription from specific target promoters upon binding to cis-acting DNA sequence elements. The v-erbA oncogene of avian erythroblastosis virus (AEV) encodes a ligand-independent version of this nuclear receptor. The v-erbA product inhibits terminal differentiation of avian erythroblasts, presumably by affecting the transcription of specific genes. We show here that the c-erbA-encoded nuclear receptor (p46c-erbA) is phosphorylated on serine residues on two distinct sites. One of these sites, defined by the limit tryptic phosphopeptide 28SSQCLVK, is retained on the v-erbA-encoded P75gag-v-erbA protein. This site is located in the amino-terminal domain of these molecules, 21 amino acids upstream of the DNA-binding region. Phosphorylation of this site in both p46c-erbA and P75gag-v-erbA is enhanced 10-fold following treatment of cells with activators of either protein kinase C or cAMP-dependent protein kinase. Since cAMP-dependent protein kinase phosphorylates both p46c-erbA and P75gag-v-erbA in vitro at the same site as that observed in vivo, at least part of the cAMP-dependent phosphorylation of erbA molecules in cells could result from direct phosphorylation by this enzyme. The possible role phosphorylation may play in the function of the erbA-encoded transcriptional factors is discussed.

Alpharetrovirus↗

PubMed2002

The gene encoding Arabidopsis thaliana mitochondrial ribosomal protein S13 is a recent duplication of the gene encoding plastid S13.

A gene encoding mitochondrial S13 is generally present in the mitochondrial genome of higher plants, but is lacking from the Arabidopsis thaliana mitochondrial genome. Previous research has failed to identify a nuclear gene capable of encoding a mitochondrial S13 protein or the protein itself. Doubts have even been raised as to whether a mitochondrial S13 exists in Arabidopsis. Here, we show that the nuclear gene encoding the plastid S13 has been partially duplicated in A. thaliana, such that the copy has lost the exon encoding the plastid transit peptide and acquired a sequence capable of encoding a mitochondrial targeting sequence. The two S13 sequences were fused to green fluorescent protein and shown to be targeted to plastids and mitochondria respectively.

Amino Acid Sequence↗

PubMed1994

Characterization of a cDNA encoding a manganese peroxidase from Phanerochaete chrysosporium: genomic organization of lignin and manganese peroxidase-encoding genes.

Two heme proteins, manganese peroxidase (MnP) and lignin peroxidase (LiP), play key roles in the fungal depolymerization of lignin. Many cDNA and genomic clones encoding these peroxidases have been published. We report here on the cDNA lambda MP-2 encoding the MnP isozyme H3 from Phanerochaete chrysosporium strain BKM-F-1767. We also demonstrate that the MnP-encoding gene, lambda MP-1, encoding isozyme H4, and lambda MP-2 reside on separate chromosomes from each other and from the LiP-encoding genes. From these results, it is apparent that lambda MP-2 is not linked to lambda MP-1 or other genes believed to be involved in lignin depolymerization, such as the LiP and glyoxal oxidase.

Amino Acid Sequence↗

PubMed2006

The cell-mediated immune response induced by plasmid encoding bovine herpesvirus 1 glycoprotein B is enhanced by plasmid encoding IL-12 when delivered intramuscularly or by gene gun, but not after intradermal injection.

Bovine herpesvirus 1 (BHV-1) causes respiratory and genital infections in cattle. Previously we demonstrated that a DNA vaccine encoding a truncated, secreted form of BHV-1 glycoprotein B (tgB) induces cytotoxic T lymphocyte (CTL) responses in C3H mice. In this study we investigated the potential of interleukin 12 (IL-12) to further enhance the CTL response. C3H mice were immunized with a plasmid encoding tgB or with plasmids encoding tgB and murine IL-12. When the plasmid encoding tgB was delivered intramuscularly or epidermally by a gene gun, co-administration with IL-12 plasmid stimulated the synthesis of more IgG2a, the production of higher levels of IFN-gamma, and more effective killing by CTLs. In contrast, after intradermal delivery no effect of co-administration of IL-12 encoding plasmid was observed. Further investigation suggested that antigen and IL-12 need to be expressed in the draining lymph nodes, where IL-12 can have a direct effect on T cells.

Animals↗

PubMed1997

The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species.

We have previously identified distinct nuclear and mitochondrial isoforms of dUTPase in human cells, reporting the cDNA sequence of the nuclear isoform (DUT-N). We now report a cDNA corresponding to the mitochondrial isoform (DUT-M). The DUT-M cDNA contains an 252-amino acid open reading frame, encoding a protein with a predicted Mr of 26,704. The amino-terminal region of the protein contains an arginine-rich, 69-residue mitochondrial targeting presequence that is absent in the mature protein. In vitro transcription and translation of the DUT-M cDNA results in the production of a precursor protein with an apparent molecular mass of 31 kDa as judged by SDS-polyacrylamide gel electrophoresis. The DUT-M precursor is enzymatically active and immunoreacts with a dUTPase-specific monoclonal antibody. Mitochondrial import and processing studies demonstrate that the DUT-M precursor is processed into a 23-kDa protein and imported into mitochondria in vitro. Isoelectric focusing experiments demonstrate that the DUT-N has a pI of 6.0, while the processed form of DUT-M has a more basic pI of 8.1, measurements that are in agreement with predicted values. Studies aimed at understanding the expression of these isoforms were performed utilizing quiescent and replicating 34Lu human lung fibroblasts as a model cell culture system. Northern blot analysis, employing an isoform-specific probe, demonstrates that DUT-N and DUT-M are encoded by two distinct mRNA species of 1.1 and 1.4 kilobases, respectively. Western and Northern blot analysis reveal that DUT-M protein and mRNA are expressed in a constitutive fashion, independent of cell cycle phase or proliferation status. In contrast, DUT-N protein and mRNA levels are tightly regulated to coincide with nuclear DNA replication status. Because DUT-N and DUT-M have identical amino acid and cDNA sequences in their overlapping regions, we set out to determine if they were encoded by the same gene. The 5' region of the gene encoding dUTPase was isolated and characterized by a combination of Southern hybridization and DNA sequencing. These analyses demonstrate that the dUTPase isoforms are encoded by the same gene with isoform-specific transcripts arising through the use of alternative 5' exons. This finding represents the first example in humans of alternative 5' exon usage to generate differentially expressed nuclear and mitochondrial specific protein isoforms.

Amino Acid Sequence↗

PubMed2001

The typically mitochondrial DNA-encoded ATP6 subunit of the F1F0-ATPase is encoded by a nuclear gene in Chlamydomonas reinhardtii.

The atp6 gene, encoding the ATP6 subunit of F(1)F(0)-ATP synthase, has thus far been found only as an mtDNA-encoded gene. However, atp6 is absent from mtDNAs of some species, including that of Chlamydomonas reinhardtii. Analysis of C. reinhardtii expressed sequence tags revealed three overlapping sequences that encoded a protein with similarity to ATP6 proteins. PCR and 5'- and 3'-RACE were used to obtain the complete cDNA and genomic sequences of C. reinhardtii atp6. The atp6 gene exhibited characteristics of a nucleus-encoded gene: Southern hybridization signals consistent with nuclear localization, the presence of introns, and a codon usage and a polyadenylation signal typical of nuclear genes. The corresponding ATP6 protein was confirmed as a subunit of the mitochondrial F(1)F(0)-ATP synthase from C. reinhardtii by N-terminal sequencing. The predicted ATP6 polypeptide has a 107-amino acid cleavable mitochondrial targeting sequence. The mean hydrophobicity of the protein is decreased in those transmembrane regions that are predicted not to participate directly in proton translocation or in intersubunit contacts with the multimeric ring of c subunits. This is the first example of a mitochondrial protein with more than two transmembrane stretches, directly involved in proton translocation, that is nucleus-encoded.

Adenosine Triphosphatases↗

PubMed1998

Coexistence of nuclear DNA-encoded tRNAVal(AAC) and mitochondrial DNA-encoded tRNAVal(UAC) in mitochondria of a liverwort Marchantia polymorpha.

The liverwort Marchantia polymorpha mitochondrial DNA encodes almost all tRNAs required for mitochondrial translation except for the isoleucine (AUU, AUC) and threonine (ACA, ACG) codons, while the missing tRNAs are supplied in part by the nucleus and imported in mitochondria. In this paper, we report a finding of two radically different nuclear tRNAVal(AAC) genes and import of the corresponding tRNA isoacceptors in M.polymorpha mitochondria. This finding is surprising since the mtDNA encodes the gene for tRNAVal(UAC), which alone was considered sufficient for translating all four valine codons GUN by the U/N wobble mechanism. The present results suggest for the first time that the import of ncDNA-encoded tRNAs may result in decoding overlaps in plant mitochondria. The coexistence of nuclear DNA-encoded tRNAVal(AAC) and mitochondrial DNA-encoded tRNAVal(UAC) in liverwort mitochondria and the significance for the decoding mechanism as well as evolution of tRNA import are discussed.

Biological Transport↗

PubMed2000

The locus of enterocyte effacement (LEE)-encoded regulator controls expression of both LEE- and non-LEE-encoded virulence factors in enteropathogenic and enterohemorrhagic Escherichia coli.

Regulation of virulence gene expression in enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic E. coli (EHEC) is incompletely understood. In EPEC, the plasmid-encoded regulator Per is required for maximal expression of proteins encoded on the locus of enterocyte effacement (LEE), and a LEE-encoded regulator (Ler) is part of the Per-mediated regulatory cascade upregulating the LEE2, LEE3, and LEE4 promoters. We now report that Ler is essential for the expression of multiple LEE-located genes in both EPEC and EHEC, including those encoding the type III secretion pathway, the secreted Esp proteins, Tir, and intimin. Ler is therefore central to the process of attaching and effacing (AE) lesion formation. Ler also regulates the expression of LEE-located genes not required for AE-lesion formation, including rorf2, orf10, rorf10, orf19, and espF, indicating that Ler regulates additional virulence properties. In addition, Ler regulates the expression of proteins encoded outside the LEE that are not essential for AE lesion formation, including TagA in EHEC and EspC in EPEC. delta ler mutants of both EPEC and EHEC show altered adherence to epithelial cells and express novel fimbriae. Ler is therefore a global regulator of virulence gene expression in EPEC and EHEC.

Amino Acid Sequence↗

PubMed1988

A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site.

We describe the results of a study designed to identify cDNAs encoding Ca2+-transporting ATPases and other cation-transporting ATPases of the aspartylphosphate class. Rat brain, kidney, and stomach cDNA libraries were screened with an oligonucleotide hybridization probe corresponding to a 23-amino acid sequence from part of the ATP-binding site of the sarcoplasmic reticulum Ca-ATPase. This procedure resulted in the isolation of cDNAs encoding (i) the plasma membrane Ca-ATPase, (ii) an apparent Ca-ATPase that exhibits high amino acid similarity to the sarcoplasmic reticulum Ca2+ pumps, (iii) a transport ATPase of unknown ion specificity and (iv) two Ca-ATPase isoforms encoded by the gene for the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase. Several isoforms of the Na,K-ATPase and gastric H,K-ATPase that had been characterized previously were also identified. The complete nucleotide sequences have been determined for the two classes of cDNA derived from alternatively spliced transcripts of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. One of these cDNAs, isolated from the stomach library, encodes a Ca-ATPase that is identical to the skeletal muscle enzyme. The second class of cDNA, found in brain, kidney, and stomach libraries, is identical to that of the slow-twitch isoform throughout much of its length but encodes an alternative C terminus and has a different 3'-untranslated sequence. Whereas the muscle isoform consists of 997 amino acids and terminates with the sequence Ala-Ile-Leu-Glu, the second isoform is 1043 amino acids in length due to the replacement of these last 4 amino acids with a 50-amino acid sequence that contains a potential transmembrane domain followed by a consensus sequence for an N-linked glycosylation site.

Adenosine Triphosphatases↗

PubMed1998

[A case of cerebral venous angioma detected by slow velocity-encoding phase contrast MRA: appropriate determination of velocity encode].

We report a 86-year-old woman who has been diagnosed as cerebral venous angioma by slow velocity-encoding phase contrast magnetic resonance angiography (MRA). She had developed headache for one month. T1- and T2-weighted images showed a flow void sign in the right cerebellum with gadolinium enhancement. MRA using time-of-flight sequence revealed no abnormal vascular structures. Conventional phase contrast MRA (velocity encode, 40 or 60 cm/sec) did not disclose obvious vascular abnormalities. However, slow velocity-encoding (20 cm/sec) phase contrast MRA demonstrated a well-demarcated venous angioma in the right transverse sinus. Our results of MRAs suggest that velocity encode is a crucial factor for detection of venous angioma on phase contrast MRA. Slow velocity-encoding phase contrast MRA is a beneficial tool for evaluation of venous malformations, such as venous angioma.

Aged↗

PubMed2005

Co-vaccination with adeno-associated virus vectors encoding human papillomavirus 16 L1 proteins and adenovirus encoding murine GM-CSF can elicit strong and prolonged neutralizing antibody.

Non-infectious human papillomavirus-like particles (VLPs), encoded by the major capsid gene L1, have been shown to be effective as vaccines to prevent cervical cancer. We have developed the genetic immunization of the L1 gene to induce a neutralizing antibody. We constructed and generated a recombinant adeno-associated virus encoding human papillomavirus (HPV) 16 L1 protein that could form virus-like particles in transduced cells. Previous reports have demonstrated that the formation of VLP is necessary to induce high titers of neutralizing antibodies to protect an animal from viral challenge. Therefore, we carried out a single intramuscular (i.m.) injection with recombinant adeno-associated virus encoding HPV-16 L1 protein (rAAV-16L1) in BALB/c mice, which ultimately produced stronger and more prolonged neutralizing L1 antibodies, when compared to the DNA vaccine. Immunohistochemistry showed that the accumulation of antigen presenting cells, such as macrophages and dendritic cells, in rAAV-16L1 and L1 DNA-injected muscle fibers may be due to the L1 protein expression, but not to AAV infection. When compared to the L1 VLP vaccine, however, the titers of neutralizing L1 antibodies induced by VLP were higher than those induced by rAAV-16L1. Co-vaccinating with rAAV-16L1 and adenovirus encoding murine GM-CSF (rAAV-16L1/rAd-mGM-CSF) induced comparable higher levels of neutralizing L1 antibodies with those of VLP. This implies that a single i.m. co-injection with rAAV-16L1/rAd-mGM-CSF can achieve the same vaccine effect as a VLP vaccine requiring 3 booster injections.

Adenoviridae↗

PubMed2007

Improved cine displacement-encoded MRI using balanced steady-state free precession and time-adaptive sensitivity encoding parallel imaging at 3 T.

Cine displacement-encoded MRI is a promising modality for quantifying regional myocardial function. However, it has two major limitations: low signal-to-noise ratio (SNR) and data acquisition efficiency. The purpose of this study was to incrementally improve the SNR and the data acquisition efficiency of cine displacement-encoded MRI through the combined use of balanced steady-state free precession (b-SSFP) imaging, 3T imaging, echo-combination image reconstruction, and time-adaptive sensitivity encoding (TSENSE) parallel imaging. Phantom experiments were performed to empirically determine the optimal excitation angle (alpha) and to estimate the measurement errors in the presence of 130 Hz peak-to-peak static magnetic field (B0) variation. The optimal alpha was determined to be 20 degrees . The intrinsic phase correction in the echo-combination effectively reduced the phase error, which produced small displacement errors (0.11 versus 0.11 mm) and negligible strain errors (-0.001 versus -0.002). Six healthy volunteers were imaged in three short-axis levels of the heart to evaluate the SNR and the relative accuracy of strain calculations. Compared with the 24-heartbeat cine echo-planar imaging acquisition, the 24-heartbeat non-accelerated b-SSFP acquisition yielded approximately 65% higher SNR, and the 12-heartbeat twofold accelerated b-SSFP acquisition yielded approximately 28% higher SNR. The 12-heartbeat twofold accelerated b-SSFP acquisition yielded functional maps with spatial resolution of 3.6 x 3.6 mm, temporal resolution of 35 ms, and relatively high SNR (31.2 +/- 5.4 at end diastole; 19.9 +/- 3.6 at end systole; 10.3 +/- 1.1 at late diastole; mean +/- SD). The left ventricular strain values between the non-accelerated and twofold accelerated b-SSFP acquisitions correlated strongly (slope = 0.99; bias = 0.00; R2 = 0.91) and were in excellent agreement. The combined implementation of b-SSFP imaging, 3T imaging, echo-combination image reconstruction, and TSENSE parallel imaging can be used to incrementally improve the cine displacement-encoded MRI pulse sequence.

Adult↗

PubMed1988

Nucleotide sequences of cDNAs encoding four complete nuclear-encoded plastid ribosomal proteins.

The nucleotide sequences of four pea nuclear-encoded plastid ribosomal protein cDNAs have been determined. These cDNAs were shown to encode the complete precursor proteins. The transit sequences of the encoded proteins are similar to the transit sequences of other imported proteins being rich in serine and/or threonine and lacking aspartic and glutamic acid. The transit sequences do not, however, have any apparent amino acid sequence similarity with one another or with the transit sequences of other imported proteins. The derived amino acid sequences of the plastid ribosomal proteins were compared to the amino acid sequences of other ribosomal proteins. Significant amino acid sequence similarity was found between Escherichia coli ribosomal proteins L9 and L24 and two of the nuclear-encoded pea plastid ribosomal proteins.

Amino Acid Sequence↗

PubMed1996

Isolation of the vma-6 gene encoding a 41 kDa subunit of the Neurospora crassa vacuolar ATPase, and an adjoining gene encoding a ribosome-associated protein.

The vma-6 gene, encoding a membrane-associated subunit of the vacuolar H+-ATPase from Neurospora crassa, was cloned and sequenced. The gene contains three small introns and encodes a protein of 41 005 Da. When compared with homologous polypeptides from other species, the N. crassa protein contains a unique glycine-rich region. Three conserved cysteine residues, previously unrecognized, have been identified. An unrelated gene encoding a protein of 31 701 Da was found 2.1 kb downstream of vma-6. The second appears to encode the N. crassa homolog of a ribosome-associated protein identified previously in several plant and mammalian cells, and was named rap-1.

Adenosine Triphosphatases↗

PubMed1993

Encoding ability is preserved in amnesia: evidence from a direct test of encoding.

The encoding ability of 17 amnesics of mixed aetiology and 17 matched normal controls was assessed directly using a novel procedure. On two separate occasions, subjects were shown 60 complex drawings each containing six pictures. On one occasion each drawing was shown for 6 sec, and on the other occasion it was shown for 25 sec. Immediately after presentation of each drawing subjects were asked a single unpredictable question about picture colours, location, size or semantic category. Amnesics performed normally in the 6-sec exposure condition indicating that all of the tested kinds of information were encoded at a normal rate. Performance in this condition correlated with short-term, but not long-term memory in the amnesics indicating that it depended largely on encoding and short-term memory. However, the amnesics were impaired in the 25-sec condition where performance should have depended on (long-term) memory abilities at which they were impaired. The results are inconsistent with available encoding deficit accounts of amnesia.

Adult↗

PubMed1983

The operon that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12.

The sigma subunit of E. coli RNA polymerase is encoded by the rpoD gene. Within the sequence upstream from rpoD, we have identified the structural genes rpsU and dnaG, which encode the 30S ribosomal protein S21 and DNA primase, respectively. The three genes are in the order rpsU, dnaG rpoD, and are all encoded by the same DNA strand. Analysis of in vivo transcripts from this region shows that these genes are all within the same operon. By correlating the 5' and 3' ends of in vivo transcripts with our DNA sequence, we have identified several regulatory features of the operon. These features include tandem promoters upstream from rpsU, a terminator between rpsU and dnaG, an RNA processing site separating dnaG and rpoD, and the operon terminator just downstream from rpoD. Immediately upstream of the operon promoters is an active promoter for an unidentified gene. We discuss the regulatory significance of the operon features and the biological significance of an operon encoding proteins essential for translation, replication and transcription.

Bacterial Proteins↗