The mapping of genes for spore formation on the chromosome of Bacillus licheniformis

1970 ◽  
Vol 16 (7) ◽  
pp. 595-600 ◽  
Author(s):  
Marvin Rogolsky
Keyword(s):  
Genetic Map ◽  
Bacillus Licheniformis ◽  
Ethyl Methanesulfonate ◽  
Spore Formation ◽  
Linkage Data ◽  
Early Function ◽  
Reference Markers

A total of 59 asporogenous mutants of Bacillus licheniformis were isolated after treatment with nitrosoguanidine or ethyl methanesulfonate. Forty-one of the 59 asporogenous sites were mapped by SP-15 mediated transduction on an abbreviated genetic map of B. licheniformis which contained 12 reference markers. Linkage data revealed that genes for sporulation occupied at least five separate and distinct areas of the chromosome. B. licheniformis was noted to resemble B. subtilis in that most of the spore genes in both species mapped in a cluster to the left of an identical sequence of terminal auxotrophic markers. The terminal spore cluster in B. licheniformis, as in B. subtilis, contained a locus which when defective, blocked the synthesis of a protease believed to regulate an early function of spore formation.

Antibiotic Production as a Function of Spore Formation in Bacillus licheniformis

Nature ◽  
1959 ◽  
Vol 184 (4694) ◽  
pp. 1256-1257 ◽  
Author(s):  
ROBERT W. BERNLOHR ◽  
G. D. NOVELLI
Keyword(s):  
Bacillus Licheniformis ◽  
Antibiotic Production ◽  
Spore Formation

A genetic map of chromosome 19 based on family linkage data

1985 ◽  
Vol 49 (3) ◽  
pp. 181-187 ◽  
Author(s):  
S. L. SHERMAN ◽  
S. P. BALL ◽  
E. B. ROBSON
Keyword(s):  
Genetic Map ◽  
Linkage Data ◽  
Chromosome 19

Microanatomy of the Periplasm of Bacillus Licheniformis

1971 ◽  
Vol 29 ◽  
pp. 262-263
Author(s):  
B.K. Ghosh
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Bacillus Licheniformis ◽  
External Environment ◽  
Permeability Barrier ◽  
Periplasmic Space ◽  
Modified Technique ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

The genetic map maker

Nature ◽  
2007 ◽  
Author(s):  
Alison Abbott
Keyword(s):  
Genetic Map

XYLANASE, AN ENVIRONMENTALLY FRIENDLY BLEACHING AGENT FOR PULP AND PAPER: Characterization And Stabilization Study Of Bacillus licheniformis I-5 CRUDE Xylanase

2018 ◽  
Vol 7 (3) ◽  
Author(s):  
Budiasih Wahyuntari., dkk
Keyword(s):  
Thermal Stability ◽  
Bacillus Licheniformis ◽  
Hot Spring ◽  
Sodium Dodecyl ◽  
Luria Broth ◽  
Crude Enzyme ◽  
Half Time ◽  
Triton X100 ◽  
Sds Page ◽  
Xylanolytic Enzymes

Isolate I-5 was isolated from Ciseeng hot spring, West Java and was identified as Bacillus licheniformis I-5. The isolate produces extracellular xylanolytic enzymes on Oatspelt containing Luria broth agar medium. Optimal activity of the crude enzyme was  observed at 50ºC and pH 7. The effect of sodium dodecyl sulphate, b-mercaptoethanol and Triton-X100 were observed. Incubating the crude enzyme in 1.5% SDS and 1.5% b-mercaptoethanol at 50oC for 90 minutes then adding Triton-X100 at final concentration of 3.5% for 45 minutes only reduced 5.75% of the initial enzyme activity. SDS/PAGE and zymogram analysis showed that at least two xylanolytic enzymes presence in the crude enzyme. The molecular weight of the enzyme was estimated about 127 and 20kD. The enzyme hydrolysed xylan into xylobiose, xylotriose and other longer xylooligosaccharides. Thermal stability of the crude enzyme was observed at 50, 60, and 70oC and pH 7 and 8. The results showed that the half time of the crude enzyme incubated at 50, 60, and 70oC pH 7 was 2 hours 55 minutes; 2 hours 33 minutes and 1 hour 15 minutes respectively. The half time at 50, 60 and 70oC, pH 8 was 2 hours 48 minutes; 1 hour 22 minutes and 1 hour 9 minutes respectively.keywords: Xilanase, Bacillus licheniformis I-5, thermal stability

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