Crown Gall Specific Gene Products: Octopine and Nopaline Synthase

1980 ◽  
pp. 489-496
Author(s):  
J. D. Kemp ◽  
E. Hack ◽  
D. W. Sutton
Keyword(s):  
Crown Gall ◽  
Specific Gene ◽  
Gene Products

scholarly journals Transcription of Candidate Virulence Genes ofHaemophilus ducreyi during Infection of Human Volunteers

2001 ◽  
Vol 69 (3) ◽  
pp. 1483-1487 ◽  
Author(s):  
Robert E. Throm ◽  
Stanley M. Spinola
Keyword(s):  
Experimental Infection ◽  
Virulence Genes ◽  
Human Model ◽  
Specific Gene ◽  
Gene Products ◽  
Virulence Determinants ◽  
Reverse Transcription Pcr ◽  
Human Volunteers

ABSTRACT Haemophilus ducreyi expresses several putative virulence factors in vitro. Isogenic mutant-to-parent comparisons have been performed in a human model of experimental infection to examine whether specific gene products are involved in pathogenesis. Several mutants (momp, ftpA, losB, lst, cdtC, and hhdB) were as virulent as the parent in the human model, suggesting that their gene products did not play a major role in pustule formation. However, we could not exclude the possibility that the gene of interest was not expressed during the initial stages of infection. Biopsies of pustules obtained from volunteers infected with H. ducreyiwere subjected to reverse transcription-PCR. Transcripts corresponding to momp, ftpA, losB, lst, cdtB, and hhdA were expressed in vivo. In addition, transcripts for other putative virulence determinants such as ompA2, tdhA, lspA1, andlspA2 were detected in the biopsies. These results indicate that although several candidate virulence determinants are expressed during experimental infection, they do not have a major role in the initial stages of pathogenesis.

Dimerization through the helix-loop-helix motif enhances phosphorylation of the transcription activation domains of myogenin

1994 ◽  
Vol 14 (9) ◽  
pp. 6232-6243
Author(s):  
J Zhou ◽  
E N Olson
Keyword(s):  
Transcriptional Activity ◽  
Transcription Activation ◽  
Bhlh Protein ◽  
Specific Gene ◽  
Phosphorylation Sites ◽  
Gene Products ◽  
Activation Domains ◽  
Helix Loop Helix ◽  
Carboxyl Terminal ◽  
Bhlh Proteins

The muscle-specific basic helix-loop-helix (bHLH) protein myogenin activates muscle transcription by binding to target sequences in muscle-specific promoters and enhancers as a heterodimer with ubiquitous bHLH proteins, such as the E2A gene products E12 and E47. We show that dimerization with E2A products potentiates phosphorylation of myogenin at sites within its amino- and carboxyl-terminal transcription activation domains. Phosphorylation of myogenin at these sites was mediated by the bHLH region of E2A products and was dependent on dimerization but not on DNA binding. Mutations of the dimerization-dependent phosphorylation sites resulted in enhanced transcriptional activity of myogenin, suggesting that their phosphorylation diminishes myogenin's transcriptional activity. The ability of E2A products to potentiate myogenin phosphorylation suggests that dimerization induces a conformational change in myogenin that unmasks otherwise cryptic phosphorylation sites or that E2A proteins recruit a kinase for which myogenin is a substrate. That phosphorylation of these dimerization-dependent sites diminished myogenin's transcriptional activity suggests that these sites are targets for a kinase that interferes with muscle-specific gene expression.

Localization and Visualization of Specific Gene Products in Fungal Plant Pathogens

2000 ◽  
Vol 6 (S2) ◽  
pp. 680-681 ◽  
Author(s):  
T. M. Bourett ◽  
K. J. Czymmek ◽  
T. M. Dezwaan ◽  
J. A. Sweigard ◽  
R. J. Howard
Keyword(s):  
Fungal Pathogens ◽  
Plant Pathogens ◽  
Protein Localization ◽  
Infected Plant ◽  
Cell Interaction ◽  
Specific Gene ◽  
Gene Products ◽  
Tem Analysis ◽  
Fungal Plant Pathogens ◽  
Plant Pathogenesis

Specific gene products of both pathogens and hosts have been implicated as decisive elements during plant pathogenesis. While expression of some of these genes is constitutive, that of others is likely ephemeral and activated only during a particular stage of the interaction. Because the relative timing of expression may be critical, transcription and translation have often been addressed by extracting mRNA and proteins from infected plant tissue. This approach, however, cannot readily detect proteins of low abundance in bulk samples nor offer much useful information on cell-cell interaction. Only a cytological analysis that employs microscopy can resolve the temporal and spatial details of gene expression. Typically, such protein localization studies have required specific antibodies, but these large probe molecules do not diffuse into living or conventionally fixed cells of either fungal pathogens or plant hosts. For TEM analysis, these permeability-imposed limitations have been reduced by thin sectioning to render accessible antibody binding sites.

scholarly journals Dexamethasone-dependent inhibition of differentiation of C2 myoblasts bearing steroid-inducible N-ras oncogenes.

1988 ◽  
Vol 106 (6) ◽  
pp. 2127-2137 ◽  
Author(s):  
L A Gossett ◽  
W Zhang ◽  
E N Olson
Keyword(s):  
Gene Expression ◽  
Growth Factors ◽  
Specific Gene ◽  
Dependent Manner ◽  
Gene Products ◽  
Ras Proteins ◽  
Inhibitory Effects ◽  
Specific Gene Expression ◽  
Ras Oncogenes ◽  
Inhibition Of Differentiation

ras proteins are localized to the plasma membrane where they are postulated to interact with growth factor receptors and other proximal elements in intracellular cascades triggered by growth factors. The molecular events associated with terminal differentiation of certain skeletal myoblasts are inhibited by specific polypeptide growth factors and by constitutive expression of transforming ras oncogenes. To determine whether the inhibitory effects of ras on myogenic differentiation were reversible and to investigate whether muscle-specific genes remained susceptible to ras-dependent repression in terminally differentiated myotubes, the murine myoblast cell line, C2, was transfected with a plasmid containing a mutationally activated human N-ras oncogene under transcriptional control of the steroid-sensitive promoter of the mouse mammary tumor virus long terminal repeat. Addition of dexamethasone to myoblasts bearing steroid-inducible ras oncogenes prevented myotube formation and induction of muscle creatine kinase and acetylcholine receptors. Inhibition of differentiation by dexamethasone occurred in a dose-dependent manner and was a titratable function of ras expression. In the presence of dexamethasone, myoblasts bearing steroid-inducible ras genes retained their dependence on exogenous growth factors to divide and exhibited contact inhibition of growth at confluent densities, indicating that the inhibitory effects of ras on differentiation were independent of cell proliferation. Removal of dexamethasone from N-ras-transfected myoblasts led to fusion and induction of muscle-specific gene products in a manner indistinguishable from control C2 cells. Examination of the effects of culture media conditioned by ras-transfected myoblasts on differentiation of normal C2 cells yielded no evidence for inhibition of differentiation via an autocrine mechanism. In contrast to the ability of N-ras to prevent up-regulation of muscle-specific gene products in myoblasts, induction of N-ras in terminally differentiated myotubes failed to extinguish muscle-specific gene expression. Together, these results suggest that oncogenic ras proteins reversibly activate an intracellular cascade that prevents establishment of the differentiated phenotype. The inability of ras to extinguish muscle-specific gene expression in terminally differentiated myotubes also suggests that ras may interfere with an early step in the pathway of myoblasts toward the differentiated state.

scholarly journals Dimerization through the helix-loop-helix motif enhances phosphorylation of the transcription activation domains of myogenin.

1994 ◽  
Vol 14 (9) ◽  
pp. 6232-6243 ◽  
Author(s):  
J Zhou ◽  
E N Olson
Keyword(s):  
Transcriptional Activity ◽  
Transcription Activation ◽  
Bhlh Protein ◽  
Specific Gene ◽  
Phosphorylation Sites ◽  
Gene Products ◽  
Activation Domains ◽  
Helix Loop Helix ◽  
Carboxyl Terminal ◽  
Bhlh Proteins

The muscle-specific basic helix-loop-helix (bHLH) protein myogenin activates muscle transcription by binding to target sequences in muscle-specific promoters and enhancers as a heterodimer with ubiquitous bHLH proteins, such as the E2A gene products E12 and E47. We show that dimerization with E2A products potentiates phosphorylation of myogenin at sites within its amino- and carboxyl-terminal transcription activation domains. Phosphorylation of myogenin at these sites was mediated by the bHLH region of E2A products and was dependent on dimerization but not on DNA binding. Mutations of the dimerization-dependent phosphorylation sites resulted in enhanced transcriptional activity of myogenin, suggesting that their phosphorylation diminishes myogenin's transcriptional activity. The ability of E2A products to potentiate myogenin phosphorylation suggests that dimerization induces a conformational change in myogenin that unmasks otherwise cryptic phosphorylation sites or that E2A proteins recruit a kinase for which myogenin is a substrate. That phosphorylation of these dimerization-dependent sites diminished myogenin's transcriptional activity suggests that these sites are targets for a kinase that interferes with muscle-specific gene expression.

Neurofilament proteins and human nervous system tumors.

1987 ◽  
Vol 35 (9) ◽  
pp. 999-1003 ◽  
Author(s):  
J Q Trojanowski
Keyword(s):  
Nervous System ◽  
Molecular Probes ◽  
Cytoskeletal Proteins ◽  
Diagnostic Assessment ◽  
Critical Examination ◽  
Specific Gene ◽  
Specific Class ◽  
Gene Products ◽  
Carotid Body Tumors ◽  
Human Nervous System

Neoplasms that arise in the peripheral (e.g., carotid body tumors, neuroblastomas, pheochromocytomas) or central (gangliocytomas, medulloblastomas) nervous system express a number of neuron-specific gene products. Presumably, these tumors are derived from precursor cells that are or have the potential to develop into neurons or neuron-like cells. This report provides a critical examination of the hypothesis that cytoskeletal proteins of normal neurons, in particular the neuron-specific class of intermediate filaments (neurofilaments), are present but are abnormal in neoplasms derived from neurons or neuron-like cells. The implications of these findings for understanding tumor promotion and progression, and for development of molecular probes for the diagnostic assessment of these neoplasms, are discussed.

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