Control of protein synthesis during the development of Acetabularia

Development ◽  
1971 ◽  
Vol 26 (2) ◽  
pp. 323-338
Author(s):  
Gabriel Ceron ◽  
E. Marshall Johnson

Proteins from the soluble, chloroplastic and cell membrane fractions of axenically grown Acetabularia were analysed by zone electrophoresis. Incorporation of [14C]leucine into different proteins was measured by autoradiographic analysis of the electrophoretic patterns. The protein patterns from the soluble fraction remain constant with respect to the number of detectable bands but change with respect to the relative synthetic rates at various developmental stages. The protein patterns from the membrane fraction change with respect to both the number of protein species and the relative synthetic rates. The analysis of the synthetic performance of enucleated cells revealed that most of the proteins from the soluble and the membrane fractions continue to be synthesized in the absence of the nucleus and that the changes that normally occur in the protein patterns of the membrane fraction at the time of cap formation also take place in enucleated cells. This is taken as an indication that the control of the synthesis of the proteins studied is of extranuclear nature. It was also found that chloroplasts are capable of synthesizing all the components of the chloroplastic protein spectrum at least 4 weeks after enucleation. Some of the chloroplastic proteins can also be synthesized by purified chloroplasts in extracellular conditions. The possibility of extranuclear control of protein synthesis being a rather general phenomenon during the development of Acetabularia is discussed.

1996 ◽  
Vol 74 (5) ◽  
pp. 653-658
Author(s):  
S. Pasqualini ◽  
P. Batini ◽  
L. Ederli ◽  
F. Panara ◽  
M. Antonielli

The acid phosphatase activity in the soluble, membrane, and cell wall fractions from Hordeum vulgare in dry seeds and during seedling development was investigated. The acid phosphatase activities were also assayed in barley roots and coleoptiles at different developmental stages. Electrophoretic patterns of multiple acid phosphatases in seeds, endosperms and embryos, and growing roots and coleoptiles are shown. The enzyme activity shows a rapid decrease in both roots and coleoptiles during growth. Using nondenaturing polyacrylamide gel electrophoresis, multiple acid phosphatase forms were found in all the organs examined. However, no qualitative differences in the location of bands were observed between root and coleoptile extract at various stages of development. The coleoptile cell wall fraction showed an acid phosphatase form characterized by a very low electrophoretic mobility that was not found in the soluble fraction. Keywords: barley, Hordeum vulgare L., acid phosphatase, isoforms, seedlings growth.


Development ◽  
1961 ◽  
Vol 9 (1) ◽  
pp. 202-221
Author(s):  
B. R. A. O'Brien

The embryo provides a sequence of developmental stages in which proteins both structural and enzymatic appear or become detectable for the first time in a restricted group of dividing cells. The cells or tissues can be maintained in vitro for a period that may precede and include the synthesis of a specific ‘cytoplasmic’ protein. In this way systems of protein synthesis within the cells of higher organisms can be studied during those stages in which current hypotheses suggest that some structural code is passed on from the DNA of the nucleus to the cytoplasm where the synthesis of the protein becomes maximal. Acellular preparations have contributed much to the elucidation of protein synthesis, but it is doubtful whether actual net synthesis has been obtained in systems less complex than the ‘protoplast’ developed by Spiegelman (1957). In order to study the synthesis of a specific protein it seems necessary at this stage to use whole cells.


1987 ◽  
Vol 42 (4) ◽  
pp. 353-359 ◽  
Author(s):  
Katsuyuki Tanizawa ◽  
Nobuyoshi Nakajima ◽  
Tetsuo Toraya ◽  
Hidehiko Tanaka ◽  
Kenji Soda

We have purified diol dehydrase, an adenosylcobalamin-dependent enzyme, from Klebsiella pneumoniae by two different procedures to re-investigate its protein structure; one including its extraction with detergent from the membrane fraction, and the other consisting of only chromato­graphic separations of the soluble fraction. The enzyme preparations obtained by these two methods were different in the subunit structure, but both are identical in molecular weight, and in enzymological and immunochemical properties. In addition, the enzyme preparation obtained from the membrane fraction dissociated reversibly into two dissimilar protein components (F and S) in the absence of substrate, as did the preparation from the soluble fraction. Although the subunit multiplicity of component S might be partly due to proteolytic cleavage during the enzyme purification as revealed by limited digestion with trypsin, component F is not a product of proteolytic cleavage of component S, but a primordial and essential constituent of the enzyme.


1989 ◽  
Vol 35 (3) ◽  
pp. 373-378
Author(s):  
Richard A. Nolan

The patterns of protein synthesis associated with three sequential stages in protoplast morphogenesis (spindle-shaped, early fusion sphere, and late fusion sphere protoplasts) of the fungus Entomophaga aulicae were studied using both one-dimensional gels with general protein staining and two-dimensional gels with [35S]methionine protein labelling and fluorography. A total of 332 proteins were observed with 63.5% (211) common to all three developmental stages. Of the individual totals, 3.3% (8 out of 245), 7.3% (22 out of 301), and 4.5% (13 out of 286) of the proteins were unique to the spindle-shaped, early fusion sphere, and late fusion sphere protoplasts, respectively. The molecular mass and pI distribution profiles for early fusion sphere protoplast proteins are discussed.Key words: protein synthesis, stage-specific proteins, fungal protoplasts, Entomophaga aulicae.


1962 ◽  
Vol 40 (6) ◽  
pp. 709-716 ◽  
Author(s):  
Peter B. Hill

An isolated membrane fraction of lysed protoplasts of Bacillus megaterium incorporated S35methionine and C14orotic acid into proteinaceous and ribonucleic acid material respectively.After treatment of the membrane fraction with snake venom, a reduction in S35methionine incorporation was noted. Disruption of the phospholipid components in the isolated membrane caused a similar reduction in S35methionine incorporation. Evidence presented indicated the involvement of phospholipoprotein and ribonucleic acid in protein synthesis in the membrane of B. megaterium.


1963 ◽  
Vol 41 (1) ◽  
pp. 9-18 ◽  
Author(s):  
A. T. Matheson

Two types of intracellular aminopeptidase activity are present in E. coli B. One type, present in the 'soluble' fraction, is completely inactivated by chymotrypsin or trypsin; the other, in the particulate fractions ('ribosome' and 'membrane'), is resistant to these enzymes. The 'ribosomal' peptidase activity is present partially in a latent form which becomes activated on disruption of the ribosome structure. During the transition from log phase to post-log phase growth there is a progressive increase in the specific activity of the peptidase in the 'soluble' and 'membrane' fraction and a corresponding decrease in the 'ribosome' fraction.


1956 ◽  
Vol 2 (5) ◽  
pp. 303-319 ◽  
Author(s):  
Moses Wurm ◽  
Frederick H Epstein

Abstract 1. A procedure for paper electrophoresis has been described which gives highly reproducible protein patterns with good resolution and freedom from distortions. 2. Densitometry of protein bands on paper stained with bromphenol blue or Amidoschwarz 10B reveals that the logarithm of protein concentration is proportional to optical density and that Beer's law does not apply. Electrophoretic patterns of normal human serum evaluated in this manner give values in close agreement with those obtained by moving-boundary electrophoresis. 3. Confidence limits were determined for both methods.


2006 ◽  
Vol 18 (2) ◽  
pp. 341-350 ◽  
Author(s):  
José Beltrano ◽  
Marta Guillermina Ronco ◽  
María Cecilia Arango

Water deficits cause large yield losses in wheat. Although anthesis is generally considered the most vulnerable period, water deficit during grain filling can also cause yield losses. The objective of this study was to investigate the effect of water stress and rewatering, at three different grain developmental stages, on physiological and grain filling parameters and on yield components. Wheat plants were subjected to water deficit and rewatering at the watery ripe, milk and soft dough stages. In the flag leaf, water stress decreased the relative water content, the chlorophyll and protein content and increased the leakage of solutes, at all three studied grain filling stages. Water stress at the watery ripe and milk stages reduced the final grain dry mass by 47 % and 20 %, respectively. This reduction was due to a decrease in the grain filling period and to a significant reduction in the maximum rate of grain-fill. Water stress imposed at the watery ripe stage reduced not only the linear growth phase but also its slope; grain number per spike and the 1000-kernel weight were also significantly reduced. SDS-PAGE patterns of grain proteins at the watery ripe stage did not differ between the controls, stressed or rewatered treatments. Protein patterns at the milk stage changed substantially with water stress, mainly for the high molecular weight glutenin subunits and gliadins. Three new bands were observed with apparent molecular weights of 108.5 kDa, 84.8 kDa and 63 kDa. Rewatering reverted water stress effects when it was imposed at the milk stage. Water deficit at the soft dough stage did not have any effect on protein grain patterns.


1959 ◽  
Vol 73 (2) ◽  
pp. 369-376 ◽  
Author(s):  
G D Hunter ◽  
P. Brookes ◽  
A. R. Crathorn ◽  
J. A. V. Butler

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