Studies On The Structure And Cellular Location Of Various Ribosome And Ribosomal Rna Species In The Green Alga Chlamydomonas Reinhardi

1971 ◽  
Vol 8 (1) ◽  
pp. 153-183 ◽  
Author(s):  
D. P. BOURQUE ◽  
J. E. BOYNTON ◽  
N. W. GILLHAM
Keyword(s):  
Ribosomal Rna ◽  
Gel Electrophoresis ◽  
Sucrose Gradient ◽  
Chlorophyll Synthesis ◽  
Sedimentation Velocity ◽  
Wild Type ◽  
Progressive Reduction ◽  
Lamellar System ◽  
Subunit Dissociation ◽  
Type C

Under ionic conditions effecting little or no subunit dissociation, Chlamydomonas reinhardi contains 2 major classes of ribosomes with generic sedimentation velocities of 83 and 70s and 3 minor classes with sedimentation velocities of 66, 54, and 41s. Ribosomal RNAs with sedimentation velocities of 25, 23, 18, 16 and 5s have been identified. The 70-s ribosomes are in the chloroplast and contain 23-, 16- and 5-s ribosomal RNA whereas the 83-s ribosomes are in the cytoplasm and contain 25-, 18- and 5-s ribosomal RNA. Numbers of chloroplast ribosome particles counted in electron micrographs of wild type C. reinhardi and the ac-20 and y mutants have been compared with relative amounts of 70-s ribosomes determined by sucrose gradient sedimentation and amounts of 23-, 16- and 5-s ribosomal RNA determined by gel electrophoresis. In response to reduced concentrations of magnesium the 70-s ribosomes of wild type are susceptible to a progressive reduction in sedimentation velocity whereas the 66-s ribosomes of the mutant ac-20 are not. Chlorophyll synthesis and the formation of the chloroplast lamellar system do not appear to be correlated with the relative amounts of chloroplast ribosomes.

scholarly journals REGULATION OF RIBOSOMAL RNA AND 5s RNA SYNTHESIS IN DROSOPHILA MELANOGASTER: I. BOBBED MUTANTS

Genetics ◽  
1972 ◽  
Vol 72 (2) ◽  
pp. 267-276
Author(s):  
Roberto Weinmann
Keyword(s):  
Drosophila Melanogaster ◽  
Developmental Delay ◽  
Ribosomal Rna ◽  
Gel Electrophoresis ◽  
Rna Synthesis ◽  
Rrna Synthesis ◽  
Wild Type ◽  
5S Rna ◽  
Wild Type Level

ABSTRACT Analysis of the rates and amounts of rRNA and 5s RNA synthesized in Drosophila melanogaster bobbed mutants was done by using acrylamide-gel electrophoresis. The results show that the amounts of rRNA synthesized are constant, although the rates of rRNA synthesis in bb's are reduced to 30% of the wild-type level. The rates of synthesis of 5s RNA were constant. The rate of synthesis of the two kinds of molecules that enter in equimolar amounts into the mature ribosome is non-coordinated.—The rates of rRNA synthesis were shown to be proportional to the length of the scutellar bristles, supporting the notion that in trichogen cells there is no developmental delay, but the size of the bristle depends directly on the rate of rRNA synthesis.

A Stable 44S Intermediate in the Autodigestion of 50S Ribosomal Subunits

1971 ◽  
Vol 29 ◽  
pp. 430-431
Author(s):  
John H. Nisbet ◽  
Henry S. Slayter
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Ribosomal Rna ◽  
Gel Electrophoresis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Ribosomal Subunit ◽  
Wild Type ◽  
Ribosomal Subunits ◽  
Type Strains

Wild - type strains of Escherichia coli are known to contain as many as four endogenous nucleases (Ref. 1). These are commonly found associated with the ribosomes after extraction from the cell, but may be removed, with the exception of RNase IV, by washing the ribosomes in NH4Cl (at 0.2 M and higher concentrations). We have examined the effect of these nucleases on the 50S ribosomal subunit of one wild-type strain, K12 (Hfr 3000), by incubating the unwashed particles at 37° in the presence of varying magnesium concentrations.At 10-4 molar magnesium (slower at 10-3 molar), the 50S particle is converted to a species sedimenting at about 44S. About 20% of the total O.D260 is liberated at the same time. Continued incubation leads to the release of more O.D260 material while the RNA remaining in the 44S (Fig. 1) particle is progressively cleaved, eventually to the point where it consists of one principal fragment of molecular weight 0.42 x 106 daltons and several lesser fragments. The ribosomal RNA and proteins have been characterized by acrylamide gel electrophoresis.

scholarly journals Purification of argininosuccinase from Neurospora and comparison of some properties of the wild-type enzyme and an enzyme formed by inter-allelic complementation

1966 ◽  
Vol 8 (2) ◽  
pp. 243-252 ◽  
Author(s):  
Brian B. Cohen ◽  
John O. Bishop
Keyword(s):  
Molecular Weight ◽  
Calcium Phosphate ◽  
Gel Electrophoresis ◽  
Sucrose Gradient ◽  
Starch Gel Electrophoresis ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Analytical Centrifugation ◽  
Starch Gel ◽  
Kinetics Of

Argininosuccinase has been purified from wild-type Neurospora crassa, strain ST.A. The purified enzyme, which is homogeneous by the criteria of analytical centrifugation and starch-gel electrophoresis, has a molecular weight of about 175,000. The enzyme has also been partially purified from a heterokaryon between the arg-10 mutant stocks B317–9–9a and 402–3a.The reaction kinetics of the two enzymes were compared in several respects, and they were found to be indistinguishable. The enzymes were also indistinguishable by starch-gel electrophoresis, and sedimented at the same rate through a sucrose gradient. It seems likely, however, that the enzymes do differ physically since they showed different affinities for both calcium phosphate gel and hydroxylapatite during purification.

Proteomic Analysis of Leaves of the Chlorophyll-Deficient Wheat Mutant Mt6172 and Its Wild-Type through 2D-Difference Gel Electrophoresis

2013 ◽  
Vol 38 (9) ◽  
pp. 1592-1606 ◽  
Author(s):  
Su-Jie SONG ◽  
Jia-Yu GU ◽  
Hui-Jun GUO ◽  
Lin-Shu ZHAO ◽  
Shi-Rong ZHAO ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Wild Type ◽  
Difference Gel Electrophoresis ◽  
Wheat Mutant

scholarly journals DIFFERENTIATION OF DROSOPHILA CELLS LACKING RIBOSOMAL DNA, IN VITRO

Genetics ◽  
1973 ◽  
Vol 73 (3) ◽  
pp. 429-434
Author(s):  
J James Donady ◽  
R L Seecof ◽  
M A Fox
Keyword(s):  
Drosophila Melanogaster ◽  
Ribosomal Rna ◽  
Ribosomal Dna ◽  
Rna Synthesis ◽  
Wild Type ◽  
Drosophila Cells

ABSTRACT Drosophila melanogaster embryos that lacked ribosomal DNA were obtained from appropriate crosses. Cells were taken from such embryos before overt differentiation took place and were cultured in vitro. These cells differentiated into neurons and myocytes with the same success as did wild-type controls. Therefore, ribosomal RNA synthesis is not necessary for the differentiation of neurons and myocytes in vitro.

Identification of pilin pools in the membranes of Pseudomonas aeruginosa

1982 ◽  
Vol 152 (2) ◽  
pp. 687-691
Author(s):  
T H Watts ◽  
E A Worobec ◽  
W Paranchych
Keyword(s):  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Gel Electrophoresis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Wild Type ◽  
Outer Membranes

The proteins of purified inner and outer membranes obtained from Pseudomonas aeruginosa strains PAK and PAK/2Pfs were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to nitrocellulose, and treated with antiserum raised against pure pili. Bound antipilus antibodies were visualized by reaction with 125I-labeled protein A from Staphylococcus aureus. The results showed that there are pools of pilin in both the inner and outer membranes of P. aeruginosa and that the pool size in the multipiliated strain is comparable with that of the wild-type strain.

Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis

1993 ◽  
Vol 13 (3) ◽  
pp. 1464-1470
Author(s):  
S Bagrodia ◽  
S J Taylor ◽  
D Shalloway
Keyword(s):  
Kinase Activity ◽  
Tyrosine Phosphatase ◽  
Src Kinase ◽  
Indirect Evidence ◽  
Membrane Localization ◽  
Wild Type ◽  
Src Tyrosine Kinase ◽  
Amino Terminal ◽  
Membrane Bound ◽  
Type C

The chicken proto-oncoprotein c-Src is phosphorylated by p34cdc2 during mitosis concomitant with increased c-Src tyrosine kinase activity. On the basis of indirect evidence, we previously suggested that this is caused by partial dephosphorylation at Tyr-527, the phosphorylation of which suppresses c-Src kinase activity. In support of this hypothesis, we now show that treatment of cells with a protein tyrosine phosphatase inhibitor, sodium vanadate, blocks the mitotic increase in Src kinase activity. Also, we show that an amino-terminal mutation that prevents myristylation (and membrane localization) of c-Src does not interfere with the p34cdc2-mediated phosphorylations but blocks both mitotic dephosphorylation of Tyr-527 (in kinase-defective Src) and stimulation of c-Src kinase activity. Furthermore, in unsynchronized cells, the kinase activity of nonmyristylated c-Src is suppressed by 60% relative to wild-type c-Src, presumably because of increased Tyr-527 phosphorylation. Consistent with this, the Tyr-527 dephosphorylation rate measured in cell homogenates is much higher for wild-type, myristylated c-Src than for nonmyristylated c-Src. Tyr-527 phosphatase activity was primarily associated with the nonsoluble subcellular fraction. These findings suggest that the phosphatase(s) that acts on Tyr-527 is membrane bound and indicate that membrane localization of c-Src is necessary for its mitotic activation by dephosphorylation of Tyr-527.

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