A single frizzled protein has a dual function in tissue polarity

Development ◽  
1994 ◽  
Vol 120 (7) ◽  
pp. 1883-1893 ◽  
Author(s):  
R.E. Krasnow ◽  
P.N. Adler
Keyword(s):  
Dual Function ◽  
Protein Species ◽  
Hsp70 Promoter ◽  
Tissue Polarity ◽  
Genetic Mosaic ◽  
Single Protein ◽  
Genetic Epistasis ◽  
Pupal Wing ◽  
Separate Protein ◽  
Transgenic Flies

The Drosophila frizzled (fz) gene is required for the development of normal tissue polarity in the epidermis. Genetic epistasis experiments argue that fz is at the top of a regulatory hierarchy that controls the subcellular site for prehair initiation within the cells of the pupal wing (Wong and Adler, 1993; J. Cell Biol. 123, 209–221). Genetic mosaic experiments indicate that fz has both cell autonomous and cell non-autonomous functions that are separately mutable (Vinson and Adler, 1987; Nature 329, 549–551). Two species of fz mRNA have been identified, raising the question as to whether the two functions are provided by a single protein or by two separate protein species. We generated transgenic flies that express each of these mRNAs under the control of an hsp70 promoter. Only one of the transgenes (hsfzI) showed any fz activity. At 29 degrees C, the hsfzI transgene provided almost complete rescue of a null fz mutation, indicating that the protein encoded by this cDNA can fulfill both fz functions. Overexpression of the hsfzI transgene resulted in two distinct tissue polarity phenotypes depending on the time of heat shock.

c-myc can induce expression of G0/G1 transition genes

1988 ◽  
Vol 8 (8) ◽  
pp. 3080-3087
Author(s):  
C W Schweinfest ◽  
S Fujiwara ◽  
L F Lau ◽  
T S Papas
Keyword(s):  
Heat Shock ◽  
Cdna Clones ◽  
Nuclear Fraction ◽  
Mrna Levels ◽  
Protein Species ◽  
3T3 Cells ◽  
Hsp70 Promoter ◽  
Myc Oncogene ◽  
Serum Stimulation ◽  
Specific Induction

The human c-myc oncogene was linked to the heat shock-inducible Drosophila hsp70 promoter and used to stably transfect mouse BALB/c 3T3 cells. Heat shock of the transfectants at 42 degrees C followed by recovery at 37 degrees C resulted in the appearance of the human c-myc protein which was appropriately localized to the nuclear fraction. Two-dimensional analysis of the proteins of density-arrested cells which had been heat shock treated revealed the induction of eight protein species and the repression of five protein species. All of the induced and repressed proteins were nonabundant. cDNA clones corresponding to genes induced during the G0/G1 transition were used as probes to assay for c-myc inducibility of these genes. Two anonymous sequences previously identified as serum inducible (3CH77 and 3CH92) were induced when c-myc was expressed. In response to serum stimulation, 3CH77 and 3CH92 were expressed before c-myc mRNA levels increased. However, in response to specific induction of c-myc by heat shock of serum arrested cells, 3CH77 and 3CH92 mRNA levels increased after the rise in c-myc mRNA. Therefore, we hypothesize that abnormal expression of c-myc can induce genes involved in the proliferative response.

Glutamate Dehydrogenase of Pisum sativum: Heat-Dependent Interconversion of the Multiple Forms

1984 ◽  
Vol 39 (3-4) ◽  
pp. 257-260 ◽  
Author(s):  
Adelheid Ehmke ◽  
Heinz-Walter Scheid ◽  
Thomas Hartmann
Keyword(s):  
Glutamate Dehydrogenase ◽  
Direct Evidence ◽  
Molecular Forms ◽  
Stable Form ◽  
Protein Species ◽  
Multiple Forms ◽  
Single Protein ◽  
Catalytically Active ◽  
Pea Seeds ◽  
The Individual

Purified NAD-dependent glutamate dehydrogenase (EC 1.4.1.2) from pea seeds shows a pattern of seven catalytically active molecular forms. The individual forms display different heat stabilities. During incubation at 70 to 75 °C in the presence of protective agents (NADH, Ca2+, DTE) the more heat labile forms are converted into the most stable form. This result presents direct evidence that the multiple forms of pea glutamate dehydrogenase represent conform ational variants of a single protein species

Back to the future-The value of single protein species investigations

PROTEOMICS ◽  
2013 ◽  
Vol 13 (21) ◽  
pp. 3103-3105 ◽  
Author(s):  
Peter R. Jungblut
Keyword(s):  
Protein Species ◽  
Single Protein ◽  
The Future

scholarly journals c-myc can induce expression of G0/G1 transition genes.

1988 ◽  
Vol 8 (8) ◽  
pp. 3080-3087 ◽  
Author(s):  
C W Schweinfest ◽  
S Fujiwara ◽  
L F Lau ◽  
T S Papas
Keyword(s):  
Heat Shock ◽  
Cdna Clones ◽  
Nuclear Fraction ◽  
Mrna Levels ◽  
Protein Species ◽  
3T3 Cells ◽  
Hsp70 Promoter ◽  
Myc Oncogene ◽  
Serum Stimulation ◽  
Specific Induction

The human c-myc oncogene was linked to the heat shock-inducible Drosophila hsp70 promoter and used to stably transfect mouse BALB/c 3T3 cells. Heat shock of the transfectants at 42 degrees C followed by recovery at 37 degrees C resulted in the appearance of the human c-myc protein which was appropriately localized to the nuclear fraction. Two-dimensional analysis of the proteins of density-arrested cells which had been heat shock treated revealed the induction of eight protein species and the repression of five protein species. All of the induced and repressed proteins were nonabundant. cDNA clones corresponding to genes induced during the G0/G1 transition were used as probes to assay for c-myc inducibility of these genes. Two anonymous sequences previously identified as serum inducible (3CH77 and 3CH92) were induced when c-myc was expressed. In response to serum stimulation, 3CH77 and 3CH92 were expressed before c-myc mRNA levels increased. However, in response to specific induction of c-myc by heat shock of serum arrested cells, 3CH77 and 3CH92 mRNA levels increased after the rise in c-myc mRNA. Therefore, we hypothesize that abnormal expression of c-myc can induce genes involved in the proliferative response.

scholarly journals Molecular dynamics simulation reveals that switchable combinations of β-sheets underlie the prion-like properties of α-synuclein amyloids

2018 ◽  
Author(s):  
Hiroki Otaki ◽  
Yuzuru Taguchi ◽  
Noriyuki Nishida
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Prion Protein ◽  
Dynamics Simulation ◽  
Protein Species ◽  
Strain Diversity ◽  
Prion Strains ◽  
Parkinson’S Diseases ◽  
Single Protein ◽  
Β Sheets

AbstractDiversity of prion strains is one of the most mysterious traits of prions because they are mere aggregates of abnormally-folded forms of single protein species, prion protein (PrPSc), without genome. Although the strain-specific properties are hypothesized to be enciphered in the strain-specific structures of PrPSc instead of nucleotide genome, specifically what structure can code the information remains an enigma due to the incompatibility of PrPSc with structural analyses. Although the strain diversity was regarded as unique to prions, recently other disease-associated amyloids of α-synuclein (αSyn) or tau are also reported to have “strains”. As detailed structures of αSyn amyloid are already identified and the properties of mutant αSyn associated with familial Parkinson’s diseases, e.g. A53T, H50Q, and G51D, have been characterized, structure-phenotype relations of this type of amyloid could be investigated by using the αSyn amyloid as a model. Here we intensively investigated the mutant αSyn amyloids by molecular dynamics simulation to characterize influences of mutations on the structures of homo- or hetero-oligomer stacks of the amyloid. The simulations revealed directionality of the amyloid stack, remote effects of the mutations on distant β-sheets, existence of at least two switchable interfaces/amyloid cores, and distinct effects of hetero-oligomerization depending on mutation types. Collectively, those findings implied a possible mechanism of the strain diversity of the amyloids which have multiple in-register parallel β-sheets side-by-side, and support the view that their prion-like properties are inherent in the characteristic structures. We expect that the notion is also applicable to PrPSc.

Biochemical Markers in the Family Canidae.

1975 ◽  
Vol 23 (3) ◽  
pp. 411 ◽  
Author(s):  
P Clark ◽  
GE Ryan ◽  
AB Czuppon
Keyword(s):  
Genetic Markers ◽  
Biochemical Markers ◽  
Domestic Dogs ◽  
Marked Variation ◽  
Glucosephosphate Isomerase ◽  
Protein Species ◽  
Multiple Forms ◽  
The Family ◽  
Single Protein ◽  
High Degree

One quantitative and nine qualitative genetic markers were investigated in some 200 individuals of the family Canidae, including 34 breeds and species. A high degree of homogeneity was observed and only one marker, transferrin, displayed marked variation. The consistent differences were: wolf (one sample), transferrin; jackal (one sample), transferrin and glucosephosphate isomerase; foxes, albumin, transferrin and glucosephsophate isomerase. Two abnormal transferrins were observed in two siblings among six German short-haired pointers. All other markers were homogeneous, usually single protein species or multiple forms dispersed randomly through the group. The results suggest that domestic dogs and dingoes share a common pool of genes and that all canids but the foxes possess many genes in common. There are indications that the jackal and wolf may differ from other canids in some marker systems.

scholarly journals Detecting protein and post-translational modifications in single cells with iDentification and qUantification sEparaTion (DUET)

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Yandong Zhang ◽  
Changho Sohn ◽  
Seoyeon Lee ◽  
Heejeong Ahn ◽  
Jinyoung Seo ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Single Cells ◽  
Yeast Cells ◽  
Protein Species ◽  
Post Translational Modification ◽  
Histone Protein ◽  
Post Translational Modifications ◽  
Strategy Identification ◽  
Separate Protein ◽  
Identification And Quantification

AbstractWhile technologies for measuring transcriptomes in single cells have matured, methods for measuring proteins and their post-translational modification (PTM) states in single cells are still being actively developed. Unlike nucleic acids, proteins cannot be amplified, making detection of minute quantities from single cells difficult. Here, we develop a strategy to detect targeted protein and its PTM isoforms in single cells. We barcode the proteins from single cells by tagging them with oligonucleotides, pool barcoded cells together, run bulk gel electrophoresis to separate protein and its PTM isoform and quantify their abundances by sequencing the oligonucleotides associated with each protein species. We used this strategy, iDentification and qUantification sEparaTion (DUET), to measure histone protein H2B and its monoubiquitination isoform, H2Bub, in single yeast cells. Our results revealed the heterogeneities of H2B ubiquitination levels in single cells from different cell-cycle stages, which is obscured in ensemble measurements.

The Drosophila tissue polarity gene inturned acts cell autonomously and encodes a novel protein

Development ◽  
1996 ◽  
Vol 122 (3) ◽  
pp. 961-969 ◽  
Author(s):  
W.J. Park ◽  
J. Liu ◽  
E.J. Sharp ◽  
P.N. Adler
Keyword(s):  
Cdna Clone ◽  
Molecular Mapping ◽  
Hsp70 Promoter ◽  
Genetic Mosaics ◽  
Tissue Polarity ◽  
Wing Hair ◽  
A Cell ◽  
Membrane Bound ◽  
Novel Protein ◽  
Polarity Gene

Mutations in the inturned (in) gene result in abnormal wing hair polarity and in many wing cells forming two or more hairs instead of the normal single hair. We have generated genetic mosaics in a number of different experiments and find that the in gene is required in all regions of the wing and that it functions in a cell autonomous fashion. We report the molecular cloning of the in gene, the molecular mapping of in mutations and the isolation and sequencing of an in cDNA clone. The in gene encodes a novel protein whose sequence suggests it will be membrane bound. The ability of an in cDNA, the expression of which is driven by the basal activity of the hsp70 promoter to rescue an in mutation suggests that patterned expression of in is unlikely to play a role in the function of the gene.

scholarly journals Septin: a factor in plasma that opsonizes lipopolysaccharide-bearing particles for recognition by CD14 on phagocytes.

1992 ◽  
Vol 176 (3) ◽  
pp. 719-727 ◽  
Author(s):  
S D Wright ◽  
R A Ramos ◽  
M Patel ◽  
D S Miller
Keyword(s):  
Neutralizing Antibodies ◽  
Polymorphonuclear Leukocytes ◽  
Protein Species ◽  
Opsonic Activity ◽  
Coated Particles ◽  
Leukocyte Integrins ◽  
Single Protein ◽  
Normal Human ◽  
Necrosis Factor ◽  
Lps Binding

We have previously reported that lipopolysaccharide (LPS) binding protein (LBP) opsonizes endotoxin (LPS) for recognition by CD14 on phagocytes. Here we show that normal human plasma contains high titers of an activity that also binds LPS (Re, 595) and mediates recognition by CD14. Opsonization of LPS-coated particles with plasma enables the particles to be bound by phagocytes. Further, opsonization with plasma also enables subnanogram-per-milliliter concentrations of LPS to induce dramatic alterations in the function of leukocyte integrins on polymorphonuclear leukocytes and to induce secretion of tumor necrosis factor by monocytes, suggesting that opsonization by factors in plasma may be important in responses of cells to endotoxin. The opsonic activity in plasma appears distinct from LBP since it is not blocked by neutralizing antibodies against LBP. Surprisingly, the opsonic activity of plasma is not present in a single protein species, but at least two species must be combined to observe activity. Further, the opsonic activity of plasma for LPS is blocked by addition of protease inhibitors, suggesting that proteolytic activity or activities are required for opsonization. These properties are suggestive of the action of a protease cascade, but opsonic activity of plasma is not affected by blockade or depletion of either the complement or clotting cascades. We propose the name "septin" to describe this novel LPS-opsonizing activity in plasma.

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