scholarly journals Levels of Small Molecules and Enzymes in the Mother Cell Compartment and the Forespore of Sporulating Bacillus megaterium

1977 ◽  
Vol 130 (3) ◽  
pp. 1130-1138 ◽  
Author(s):  
Ravendra P. Singh ◽  
Barbara Setlow ◽  
Peter Setlow
Keyword(s):  
Small Molecules ◽  
Bacillus Megaterium ◽  
Mother Cell ◽  
Cell Compartment

scholarly journals Protein synthesis and breakdown in the mother-cell and forespore compartments during spore morphogenesis in Bacillus megaterium

1974 ◽  
Vol 144 (2) ◽  
pp. 327-337 ◽  
Author(s):  
M W Eaton ◽  
D J Ellar
Keyword(s):  
Protein Synthesis ◽  
Bacillus Megaterium ◽  
Vegetative Growth ◽  
Protein Turnover ◽  
Mother Cell ◽  
Cell Protein ◽  
Pulse Labelling ◽  
Cell Compartment ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Recently developed techniques for isolating forespores from bacilli at all stages of spore morphogenesis have been exploited to investigate the contribution of each of the two compartments of the sporulating cell to the overall pattern of protein synthesis and degradation during sporulation in Bacillus megaterium. These studies have shown: (1) that protein synthesis continues in both compartments throughout spore morphogenesis; (2) that the degradation of proteins made at all times during vegetative growth and sporulation is confined to the mother-cell compartment; (3) that proteins synthesized in the mother-cell compartment during sporulation are subsequently degraded more rapidly than proteins synthesized during vegetative growth. This rate of degradation increases the later the proteins are synthesized in the sporulation sequence. Mature spores were disrupted, and the percentage of the total protein in soluble and particulate fractions was determined. Pulse-labelling experiments were performed to investigate the extent to which the proteins of these two fractions are newly synthesized during sporulation. These data were used to calculate the extent of capture of vegetative cell protein at the time of formation of the forespore septum. The value obtained is consistent with evidence from electron micrographs and supports a model for the origin of spore protein in which there is no protein turnover in the developing forespore.

scholarly journals Assembly of Multiple CotC Forms into the Bacillus subtilis Spore Coat

2004 ◽  
Vol 186 (4) ◽  
pp. 1129-1135 ◽  
Author(s):  
Rachele Isticato ◽  
Giovanni Esposito ◽  
Rita Zilhão ◽  
Sofia Nolasco ◽  
Giuseppina Cangiano ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Posttranslational Modifications ◽  
Mother Cell ◽  
Spore Coat ◽  
Spore Surface ◽  
Subtilis Spore ◽  
Cell Compartment ◽  
Bacillus Subtilis Spore ◽  
Molecular Masses

ABSTRACT We report evidence that the CotC polypeptide, a previously identified component of the Bacillus subtilis spore coat, is assembled into at least four distinct forms. Two of these, having molecular masses of 12 and 21 kDa, appeared 8 h after the onset of sporulation and were probably assembled on the forming spore immediately after their synthesis, since no accumulation of either of them was detected in the mother cell compartment, where their synthesis occurs. The other two components, 12.5 and 30 kDa, were generated 2 h later and were probably the products of posttranslational modifications of the two early forms occurring directly on the coat surface during spore maturation. None of the CotC forms was found either on the spore coat or in the mother cell compartment of a cotH mutant. This indicates that CotH serves a dual role of stabilizing the early forms of CotC and promoting the assembly of both early and late forms on the spore surface.

scholarly journals P450BM3-Catalyzed Oxidations Employing Dual Functional Small Molecules

Catalysts ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 567 ◽  
Author(s):  
Willot ◽  
Tieves ◽  
Girhard ◽  
Urlacher ◽  
Hollmann ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hydrogen Peroxide ◽  
Cytochrome P450 ◽  
Small Molecules ◽  
Bacillus Megaterium ◽  
Cytochrome P450 Monooxygenase ◽  
Oxidation Reactions ◽  
P450 Monooxygenase ◽  
Dual Functional ◽  
Catalytic Epoxidation

A set of dual functional small molecules (DFSMs) containing different amino acids has been synthesized and employed together with three different variants of the cytochrome P450 monooxygenase P450BM3 from Bacillus megaterium in H2O2-dependent oxidation reactions. These DFSMs enhance P450BM3 activity with hydrogen peroxide as an oxidant, converting these enzymes into formal peroxygenases. This system has been employed for the catalytic epoxidation of styrene and in the sulfoxidation of thioanisole. Various P450BM3 variants have been evaluated in terms of activity and selectivity of the peroxygenase reactions.

scholarly journals LTE1 promotes exit from mitosis by multiple mechanisms

2016 ◽  
Vol 27 (25) ◽  
pp. 3991-4001 ◽  
Author(s):  
Jill E. Falk ◽  
Ian W. Campbell ◽  
Kelsey Joyce ◽  
Jenna Whalen ◽  
Anupama Seshan ◽  
...  
Keyword(s):  
Mother Cell ◽  
Regulatory Elements ◽  
Spindle Pole ◽  
Mitotic Exit ◽  
Genome Integrity ◽  
Cell Compartment ◽  
Activating Function ◽  
Spindle Pole Bodies ◽  
Mitotic Exit Network ◽  
Spindle Position

In budding yeast, alignment of the anaphase spindle along the mother–bud axis is crucial for maintaining genome integrity. If the anaphase spindle becomes misaligned in the mother cell compartment, cells arrest in anaphase because the mitotic exit network (MEN), an essential Ras-like GTPase signaling cascade, is inhibited by the spindle position checkpoint (SPoC). Distinct localization patterns of MEN and SPoC components mediate MEN inhibition. Most components of the MEN localize to spindle pole bodies. If the spindle becomes mispositioned in the mother cell compartment, cells arrest in anaphase due to inhibition of the MEN by the mother cell–restricted SPoC kinase Kin4. Here we show that a bud-localized activating signal is necessary for full MEN activation. We identify Lte1 as this signal and show that Lte1 activates the MEN in at least two ways. It inhibits small amounts of Kin4 that are present in the bud via its central domain. An additional MEN-activating function of Lte1 is mediated by its N- and C-terminal GEF domains, which, we propose, directly activate the MEN GTPase Tem1. We conclude that control of the MEN by spindle position is exerted by both negative and positive regulatory elements that control the pathway’s GTPase activity.

scholarly journals Calcium accumulation during sporulation of Bacillus megaterium KM

1978 ◽  
Vol 176 (1) ◽  
pp. 197-203 ◽  
Author(s):  
C Hogarth ◽  
D J Ellar
Keyword(s):  
Bacillus Megaterium ◽  
Concentration Gradient ◽  
Mother Cell ◽  
Dipicolinic Acid ◽  
Stage Iii ◽  
High Concentration ◽  
Cell Cytoplasm ◽  
Whole Cells ◽  
Calcium Accumulation ◽  
Km Value

Accumulation of Ca2+ in Bacilli occurs during stages IV to VI of sporulation. Ca2+ uptake into the sporangium was investigated in Bacillus megaterium KM in protoplasts prepared in stage III of sporulation and cultured to continue sporulation. These protoplasts and whole cells exhibit essentially identical Ca2+ uptake, which is compared with that of forespores isolated in stage V of sporulation. Ca2+, uptake into both sporangial protoplasts and isolated forespores occurs by Ca2+-specific carrier-mediated processes. However, protoplasts exhibit a Km value of 31 micrometer, and forespores have a Km value of 2.1 mM. Sporangial protoplasts accumulate Ca2+ against a concentration gradient. In contrast, Ca2+ uptake into isolated forespores is consistent with downhill transfer in which both rate and extent of uptake are affected by the external Ca2+ concontration. Dipicolinic acid has no effect on Ca2+ uptake by isolated forespores, apart from decreasing the external Ca2+ concentration by chelation. A model for sporulation-specific Ca2+ accumulation is proposed, in which Ca2+ is transported into the sporangium, resulting in a concentration of 3–9 mM in the mother-cell cytoplasm. This high concentration of Ca2+ enables carrier-mediated transfer down a concentration gradient into the forespore compartment, where a low free Ca2+ concentration is maintained by complexing with dipicolinic acid.

The “Pro” Sequence of the Sporulation-Specific ς Transcription Factor ςE Directs It to the Mother Cell Side of the Sporulation Septum

1999 ◽  
Vol 181 (19) ◽  
pp. 6171-6175 ◽  
Author(s):  
Jingliang Ju ◽  
W. G. Haldenwang
Keyword(s):  
Amino Acids ◽  
Transcription Factor ◽  
Bacillus Subtilis ◽  
Mother Cell ◽  
Fluorescent Protein ◽  
Amino Terminus ◽  
Cell Compartment ◽  
Intracellular Location ◽  
Specific Protease ◽  
Green Fluorescent

ABSTRACT ςE, a mother cell-specific transcription factor of sporulating Bacillus subtilis, is derived from an inactive precursor protein (pro-ςE). Activation of ςE occurs when a sporulation-specific protease (SpoIIGA) cleaves 27 amino acids from the pro-ςE amino terminus. This reaction is believed to take place at the mother cell-forespore septum. Using a chimera of pro-ςE and green fluorescent protein (GFP) to visualize the intracellular location of pro-ςE by fluorescence microscopy, and lysozyme treatment to separate the mother cell and forespore compartments, we determined that the pro-ςE::GFP signal, localized to the forespore septum prior to lysozyme treatment, is restricted to the mother cell compartment after treatment. Thus, pro-ςE::GFP had been sequestered to the mother cell side of the septum. This segregation of pro-ςE::GFP, and presumably pro-ςE, to the mother cell is likely to be the reason why ςE activity is restricted to that compartment.

scholarly journals Nutrient conditions determine the localization of Bacillus thuringiensis Vip3Aa protein in the mother cell compartment

2020 ◽  
Author(s):  
Zeyu Wang ◽  
Chunxia Gan ◽  
Jian Wang ◽  
Alejandra Bravo ◽  
Mario Soberón ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Mother Cell ◽  
Cell Compartment ◽  
Nutrient Conditions

scholarly journals Energy-dependence of calcium accumulation during sporulation of Bacillus megaterium KM

1979 ◽  
Vol 178 (3) ◽  
pp. 627-632 ◽  
Author(s):  
C Hogarth ◽  
D J Ellar
Keyword(s):  
Cell Membrane ◽  
Active Transport ◽  
Bacillus Megaterium ◽  
Mother Cell ◽  
Adenosine Triphosphatase ◽  
Nadh Oxidase ◽  
Endogenous Respiration ◽  
Facilitated Diffusion ◽  
Carbonyl Cyanide ◽  
Active Transport Process

Ca2+ accumulation and endogenous respiration of sporulating Bacillus megaterium are inhibited to the same extent by electron-transport of inhibitors and the uncoupler carbonyl cyanide p-trifluoromethoxyphenylhydrazone, suggesting that Ca2+ is accumulated by an active transport process. Forespores isolated in stage V of sporulation demonstrated Ca2+-specific carrier-mediated Ca2+ uptake, consistent with downhill transfer [Hogarth & Ellar (1978) Biochem. J. 176, 197-203]. In the present studies forespore Ca2+ uptake was unaffected by carbonyl cyanide p-trifluoromethoxyphenylhydrazone and by concentrations of respiratory inhibitor that inhibited forespore endogenous respiration by 85%. These data suggest that Ca2+ enters the isolated forespore by facilitated diffusion. Ca2+ uptake into sporulating protoplasts was completely inhibited by concentrations of respiratory inhibitors that had no effect on either Ca2+ uptake or respiration of stage-V forespores, but which resulted in inhibition of mother-cell membrane NADH oxidase. These results indicate that the mother-cell membrane is a site for active transport of Ca2+ into the sporulating cell. The effects of the adenosine triphosphatase inhibitor dicyclohexylcarbodi-imide on mother-cell membrane adenosine triphosphatase, NADH oxidase and protoplast Ca2+ uptake were examined.

scholarly journals A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables

2020 ◽  
Vol 31 (18) ◽  
pp. 1988-2001 ◽  
Author(s):  
Mikael V. Garabedian ◽  
Alison Wirshing ◽  
Anna Vakhrusheva ◽  
Bengi Turegun ◽  
Olga S. Sokolova ◽  
...  
Keyword(s):  
Mother Cell ◽  
Vesicle Transport ◽  
Cell Compartment ◽  
Bud Neck ◽  
Actin Cables

Septins and Hof1 form evenly spaced pillars at the yeast bud neck, which align, orient, and bundle actin cables entering the mother cell compartment to facilitate polarized vesicle transport.

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