Production of Antibody Fragments in the Gram-Positive Bacterium Bacillus megaterium

2010 ◽  
pp. 293-299 ◽  
Author(s):  
Miriam Steinwand ◽  
Eva Jordan ◽  
Michael Hust
2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Naomi Shimokawa-Chiba ◽  
Claudia Müller ◽  
Keigo Fujiwara ◽  
Bertrand Beckert ◽  
Koreaki Ito ◽  
...  

AbstractRescue of the ribosomes from dead-end translation complexes, such as those on truncated (non-stop) mRNA, is essential for the cell. Whereas bacteria use trans-translation for ribosome rescue, some Gram-negative species possess alternative and release factor (RF)-dependent rescue factors, which enable an RF to catalyze stop-codon-independent polypeptide release. We now discover that the Gram-positive Bacillus subtilis has an evolutionarily distinct ribosome rescue factor named BrfA. Genetic analysis shows that B. subtilis requires the function of either trans-translation or BrfA for growth, even in the absence of proteotoxic stresses. Biochemical and cryo-electron microscopy (cryo-EM) characterization demonstrates that BrfA binds to non-stop stalled ribosomes, recruits homologous RF2, but not RF1, and induces its transition into an open active conformation. Although BrfA is distinct from E. coli ArfA, they use convergent strategies in terms of mode of action and expression regulation, indicating that many bacteria may have evolved as yet unidentified ribosome rescue systems.


2019 ◽  
Author(s):  
Naomi Shimokawa-Chiba ◽  
Claudia Müller ◽  
Keigo Fujiwara ◽  
Bertrand Beckert ◽  
Koreaki Ito ◽  
...  

SummaryRescue of the ribosomes from dead-end translation complexes, such as those on truncated (non-stop) mRNA, is essential for the cell. Whereas bacteria use trans-translation for ribosome rescue, some Gram-negative species possess alternative and release factor (RF)-dependent rescue factors, which enable an RF to catalyze stop codon-independent polypeptide release. We now discover that the Gram-positive Bacillus subtilis has an evolutionarily distinct ribosome rescue factor named ResQ. Genetic analysis shows that B. subtilis requires the function of either trans-translation or ResQ for growth, even in the absence of proteotoxic stresses. Biochemical and cryo-EM characterization demonstrates that ResQ binds to non-stop stalled ribosomes, recruits homologous RF2, but not RF1, and induces its transition into an open active conformation. Although ResQ is distinct from E. coli ArfA, they use convergent strategies in terms of mode of action and expression regulation, indicating that many bacteria may have evolved as yet unidentified ribosome rescue systems.


3 Biotech ◽  
2017 ◽  
Vol 7 (5) ◽  
Author(s):  
Sikandar I. Mulla ◽  
Fuad Ameen ◽  
Preeti N. Tallur ◽  
Ram Naresh Bharagava ◽  
Manjunatha Bangeppagari ◽  
...  

2000 ◽  
Vol 351 (3) ◽  
pp. 839-839
Author(s):  
K. STEPHENSON ◽  
C. L. JENSEN ◽  
S. T. JØRGENSEN ◽  
J. H. LAKEY ◽  
C. R. HARWOOD

Author(s):  
G. M. Edidin ◽  
A. V. Brouchkov ◽  
S. G. Ignatov

From the permafrost of Mammoth Mountain in the Republic of Saha (Yakutia) samples were obtained for subsequent microbiological analysis. We were isolated Gram-positive bacterium Bacillus genus. Conducted DNA isolation and sequencing of the isolated bacteria. Phylogenetic analysis of the microorganisms from the permafrost.


1971 ◽  
Vol 17 (7) ◽  
pp. 865-869 ◽  
Author(s):  
B. Sue Criswell ◽  
Judith H. Marston ◽  
Wayne A. Stenback ◽  
S. H. Black ◽  
Herman L. Gardner

The fine structure of Haemophilus vaginalis 594 (ATCC 14018) was examined by electron microscopy, and the biochemical composition of its cell wall was determined. For comparison, similar studies were done with a Gram-positive bacterium, Bacillus megaterium KM, and a Gram-negative bacterium, Escherichia coli B. Both Haemophilus vaginalis 594 and Escherichia coli B possessed a multiple-layered cell wall containing 11 to 14 amino acids, a low mucopeptide content, and no teichoic acid. In contrast, Bacillus megaterium KM had a thick, amorphous cell wall with five amino acids, high mucopeptide content, and detectable amounts of teichoic acid. Haemophilus vaginalis 594 resembled Escherichia coli, a member of the Gram-negative group of organisms. The structural and biochemical properties of Haemophilus vaginalis, which are described in detail, may prove useful in determining the ultimate taxonomic position of this species.


Nature ◽  
10.1038/36786 ◽  
1997 ◽  
Vol 390 (6657) ◽  
pp. 249-256 ◽  
Author(s):  
F. Kunst ◽  
N. Ogasawara ◽  
I. Moszer ◽  
A. M. Albertini ◽  
G. Alloni ◽  
...  

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