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22 results on '"Bechtel, D, B."'

13. In vivo mobility of fatty acid end groups of Bacillus thuringiensis plasma membrane lipids during growth and sporulation.

Author

Bechtel, D B, Mueller, D D, Whaley, T W, and Bulla, L A

Abstract

The mobility of 13C specifically labeled branched chain end groups of iso-even fatty acids in intact, live Bacillus thuringiensis cells was studied by 13C nuclear magnetic resonance spectroscopy. This study apparently represents the first direct observation of branched chain carbon atoms in living cells. End groups were labeled using DL-[beta, delta, delta‘-13C]valine as a precursor chain initiator for iso-even fatty acid synthesis after using L-[delta, delta‘-14C]L-valine to determine optimal conditions for labeling of the membrane fatty acid end groups. Cell survival in the NMR was determined for various lengths of time at 28 and 39 degrees C. Subsequently, 13C-labeled vegetative cells, sporulating cells (three stages of development), and purified mature spores were analyzed by 13C NMR using corresponding unlabeled cells as controls. Spin lattice relaxation times (T1) were obtained for the enriched iso-branched region at 23.3 ppm and for the natural abundance peak for the glycerol backbone (carbons 1 and 3) of the membrane lipids at 61.7 ppm. The T1 of the glycerol carbons (0.08 s) did not change significantly with stage of development or temperature. The T1 of the iso-even enriched end group changed dramatically from vegetative cells (0.70s) to sporulating cells (0.28 s) at 28 degrees C. A decrease in the T1 was also observed at 39 degrees C from 0.91 s for vegetative cells to 0.54 s for sporulating cells. Accompanying the reduced mobility indicated by the T1 values, there was a general decline in the signal-to-noise ratios of identically acquired spectra as sporulation continued which culminated in the lack of discernible plasma membrane lipid resonances in purified mature spores. The progressive loss of signal appeared to have resulted from a continuous decline in the fraction of plasma membrane fatty acids with sufficient mobility to give signals above background.

Published
1985
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14. Vacuole Formation in Wheat Starchy Endosperm

Author

Bechtel, D. B., Frend, A., Kaleikau, L. A., Wilson, J. D., and Shewry, P. R.

Subjects
Vacuole Formation, Microscopy, Acid Phosphatase, Wheat, Autophagy, Cytochemistry, food and beverages, Food Science
Abstract

The formation of vacuoles in wheat (Triticum aestivum cv. Highbury) starchy endosperm cells was studied using electron microscopy. Some vacuoles were always present, even in the coenocytic cytoplasm. The first formed endosperm cells were highly vacuolated, but became filled with cytoplasm as they grew older. Various-sized pieces of cytoplasm were found in vacuoles of developing endosperm cells, probably as a result of autophagic sequestration. The membranes of the autographic vacuoles appeared to originate from the rough endoplasmic reticulum and from extensions of already-formed vacuoles. Autographic activity was confirmed by localizing the hydrolytic enzyme acid phosphatase within the vacuoles. The rough endoplasmic reticulum (RER) also stained positive for this enzyme.

Published
1989

15. The Microstructure of Wheat: Its Development and Conversion Into Bread

Author

Bechtel, D, B.

Subjects
Dough, Wheat Development, Protein Bodies, food and beverages, Golgi Apparatus, Transmission Electron Microscopy, Starch, Bread, Freeze-fracture Technique, Endoplasmic Reticulum, Endosperm, Food Science
Abstract

Wheat endosperm development has been studied in numerous laboratories. The genera 1 i zed scheme of protein body formation assembled from these data indicates that storage proteins are initially formed in the rough endoplasmic reticulum (RER). The storage proteins in RER may be processed via the Golgi apparatus into vesicles that enlarge by several mechanisms into membrane-bounded protein bodies. The prote in bodies are transported through the cytoplasm to the vacuole where they fuse with the tonoplast and deposit the protein granules into the vacuoles. The protein granules fuse with one another, lose water, and eventually become transformed into the matrix. The starchy endosperm is reduced to small particles of starch and protein during milling. These flour particles are dynamically rehydrated during dough formation. The protein forms the major structural network surrounding starch granules in doughs. The framework of bread crumb, however, is of dual composition; the protein network and a newly formed network of gelatinized starch.

Published
1985

21. Fine Structure of Succinate-Swollen Rhizobium trifolii 0403.

Author

Urban JE and Bechtel DB

Abstract

Transmission electron micrographs of glutaraldehyde- OsO(4)-fixed Rhizobium trifolii 0403 before and after cells were treated with 16.6 mM succinate showed that treated cells increased in mass by increasing cytoplasmic volume. The morphology of succinate-treated cells was identical to that of bacteroids, and the appearances of the envelope and periplasmic space were similar. The primary difference was in inclusion number and type.

Published
1984
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22. Electron microscope study of sporulation and parasporal crystal formation in Bacillus thuringiensis.

Author

Bechtel DB and Bulla LA Jr

Subjects
Bacillus thuringiensis ultrastructure, Cell Wall physiology, Inclusion Bodies ultrastructure, Morphogenesis, Organoids ultrastructure, Spores, Bacterial, Bacillus thuringiensis physiology, Inclusion Bodies physiology
Abstract

A comprehensive ultrastructural analysis of sporulation and parasporal crystal development is described for Bacillus thuringiensis. The insecticidal crystal of B. thuringiensis is initiated at the start of engulfment and is nearly complete by the time the exosporium forms. The crystal and a heretofore unobserved ovoid inclusion develop without any clear association with the forespore septum, exosporium, or mesosomes. These observations contradict previous hypotheses that the crystal is synthesized on the forespore membrane, exosporium, or mesosomes. Formation of forespore septa involves densely staining, double-membrane-bound, vesicular mesosomes that have a bridged appearance. Forespore engulfment is subpolar and also involves mesosomes. Upon completion of engulfment and the following cytoplasmic changes occur: decrease in electron density of the incipient forespore membrane; loss of bridged appearance of incipient forespore membrane; change in stainability of incipient forespore, forespore, and mother cell cytoplasms; and alteration in staining quality of plasma membrane. These changes are involved in the conversion of the incipient forespore into a forespore and reflect "commitment" to sporulation.

Published
1976
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