scholarly journals Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis.

1986 ◽  
Vol 261 (22) ◽  
pp. 10176-10181
Author(s):  
S L Wong ◽  
R H Doi
Keyword(s):  
Bacillus Subtilis ◽  
Cleavage Site ◽  
Signal Peptidase

scholarly journals Determination of cleavage sites of APendonuclease from Bacillus subtilis.

1980 ◽  
Vol 44 (7) ◽  
pp. 1713-1715
Author(s):  
Yoshihiko SAKO ◽  
Aritsune UCHIDA ◽  
Hajime KADOTA
Keyword(s):  
Bacillus Subtilis ◽  
Cleavage Sites

A deletion that includes the segment coding for the signal peptidase cleavage site delays release of Saccharomyces cerevisiae acid phosphatase from the endoplasmic reticulum

1986 ◽  
Vol 6 (2) ◽  
pp. 723-729
Author(s):  
R Haguenauer-Tsapis ◽  
M Nagy ◽  
A Ryter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Cleavage Site ◽  
Ultrastructural Localization ◽  
Signal Peptidase ◽  
Multicopy Plasmid ◽  
Wild Type ◽  
Sugar Chains ◽  
Pho5 Gene

We studied ultrastructural localization of acid phosphatase in derepressed Saccharomyces cerevisiae cells transformed with a multicopy plasmid carrying either the wild-type PHO5 gene or a PHO5 gene deleted in the region overlapping the signal peptidase cleavage site. Wild-type enzyme was located in the cell wall, as was 50% of the modified protein, which carried high-mannose-sugar chains. The remaining 50% of the protein was active and core glycosylated, and it accumulated in the endoplasmic reticulum cisternae. The signal peptide remained uncleaved in both forms. Cells expressing the modified protein exhibited an exaggerated endoplasmic reticulum with dilated lumen.

scholarly journals Determination of important enzymes and antimicrobial resistances of gram-positive haloalkaliphilic bacteria isolated from Salda Lake

2021 ◽  
Vol 38 (3) ◽  
pp. 375-382
Author(s):  
Pınar Çağlayan
Keyword(s):  
Bacillus Subtilis ◽  
Soda Lakes ◽  
Soda Lake ◽  
16S Rrna Gene Sequencing ◽  
Extreme Environment ◽  
Rrna Gene ◽  
Sequencing Analysis ◽  
Haloalkaliphilic Bacteria ◽  
Rrna Gene Sequencing

As an extreme environment, soda lakes harbor various haloalkaliphilic microorganisms. Salda Lake is one of the natural soda lake (pH˃9) in Turkey. Haloalkaliphiles are unique microorganisms in their ability to live in high alkaline and high saline conditions, and play an important role in biodegradation and bioremediation of hydrocarbons. Hence, the aims of this study were to isolate haloalkaliphilic bacteria from water sample of Salda Lake, to identify these isolates by both conventional and molecular methods, to screen their industrially important enzymes, and to investigate their antimicrobial resistance profiles. Six isolates were identified as Bacillus horneckiae, Bacillus subtilis, Bacillus paramycoides, Bacillus pumilus, Staphylococcus epidermidis, Bacillus haynesii according to 16S rRNA gene sequencing analysis. The industrially important enzymes (amylase, cellulase, pullulanase, lipase, urease, protease, caseinase, oxidase, catalase) were produced by haloalkaliphilic isolates. These enzymes maybe used in alkaline and saline industrial processes. Although Bacillus subtilis was susceptible to all antibiotics, other isolates showed resistance to at least one antibiotic. The resistance against antibiotics were found as ampicillin/sulbactam 83%, amoxycillin/clavulanic acid 83%, ampicillin 67%, mupirocin 67%, chloramphenicol 50%, tetracycline 50%, imipenem 50%, meropenem 50%, cefadroxil 17%. These bacteria may have develope resistance to antibiotics that entering their natural environment in different ways.

scholarly journals Express Method for Colorimetric Determination of Wheat Flour Contamination with Bac. Subtilis Spores

Food Industry ◽  
2020 ◽  
Vol 5 (4) ◽  
pp. 11-17
Author(s):  
Natalia Zavorokhina ◽  
Natalya Pankratyeva ◽  
Ekaterina Kryukova
Keyword(s):  
Bacillus Subtilis ◽  
Wheat Flour ◽  
Raw Materials ◽  
Wheat Bread ◽  
Colorimetric Determination ◽  
Express Method ◽  
Color Changes ◽  
Causative Agents ◽  
Potato Bread

The causative agents of potato disease are spore-forming bacteria belonging to the subspecies Bacillus subtilis ssp. mesentericus (potato bacillus), common in nature (soil, air, plants). The causative agent of potato bread disease (Bacillus subtilis ssp. mesentericus) develops in the wheat bread crumb. The affected bread loses its natural taste and aroma first, then a peculiar sweet smell appears. The crumb becomes sticky, while breaking there are mucous, stretching threads. The crumb color changes: yellow-brown and pinkish-dirty spots. When the disease develops, the bread turns into a dark layered mass with a sharp specific smell and unpleasant taste. To prevent potato bread disease (PBD), it is necessary to control raw materials and finished products in order to detect their microbiological contamination. To determine the presence of bacteria that causes potato bread disease, a man can use different methods, which are usually divided into four groups: 1) bacteriological; 2) technological; 3) biochemical and 4) physical. In all four groups of methods, there is no single method for analyzing the PBD pathogens detection, that would be easily reproduced in any laboratory and would have the correctness of evaluating the results obtained. The workers of the Food Technology Department of the Ural State University of Economics have developed an express method for colorimetric determination of wheat flour contamination with Bac. Subtilis spores based on the erythrodextrins content in it, which give a red-brown staining when interacting with an iodine solution. The advantages of the improved method for determining PBD are: a) speed and expressiveness; b) the possibility of both qualitative and quantitative determination of Bac. Subtilis in flour in order to predict the PBD occurrence in wheat flour bread.

scholarly journals Evaluation of signal peptide prediction algorithms for identification of mycobacterial signal peptides using sequence data from proteomic methods

Microbiology ◽  
2009 ◽  
Vol 155 (7) ◽  
pp. 2375-2383 ◽  
Author(s):  
Nils Anders Leversen ◽  
Gustavo A. de Souza ◽  
Hiwa Målen ◽  
Swati Prasad ◽  
Inge Jonassen ◽  
...  
Keyword(s):  
Markov Model ◽  
Signal Peptide ◽  
Cleavage Site ◽  
Hidden Markov ◽  
Signal Peptidase ◽  
Secreted Proteins ◽  
Signal Peptides ◽  
Sanger Institute ◽  
Signal Peptidase I ◽  
Peptide Prediction

Secreted proteins play an important part in the pathogenicity of Mycobacterium tuberculosis, and are the primary source of vaccine and diagnostic candidates. A majority of these proteins are exported via the signal peptidase I-dependent pathway, and have a signal peptide that is cleaved off during the secretion process. Sequence similarities within signal peptides have spurred the development of several algorithms for predicting their presence as well as the respective cleavage sites. For proteins exported via this pathway, algorithms exist for eukaryotes, and for Gram-negative and Gram-positive bacteria. However, the unique structure of the mycobacterial membrane raises the question of whether the existing algorithms are suitable for predicting signal peptides within mycobacterial proteins. In this work, we have evaluated the performance of nine signal peptide prediction algorithms on a positive validation set, consisting of 57 proteins with a verified signal peptide and cleavage site, and a negative set, consisting of 61 proteins that have an N-terminal sequence that confirms the annotated translational start site. We found the hidden Markov model of SignalP v3.0 to be the best-performing algorithm for predicting the presence of a signal peptide in mycobacterial proteins. It predicted no false positives or false negatives, and predicted a correct cleavage site for 45 of the 57 proteins in the positive set. Based on these results, we used the hidden Markov model of SignalP v3.0 to analyse the 10 available annotated proteomes of mycobacterial species, including annotations of M. tuberculosis H37Rv from the Wellcome Trust Sanger Institute and the J. Craig Venter Institute (JCVI). When excluding proteins with transmembrane regions among the proteins predicted to harbour a signal peptide, we found between 7.8 and 10.5 % of the proteins in the proteomes to be putative secreted proteins. Interestingly, we observed a consistent difference in the percentage of predicted proteins between the Sanger Institute and JCVI. We have determined the most valuable algorithm for predicting signal peptidase I-processed proteins of M. tuberculosis, and used this algorithm to estimate the number of mycobacterial proteins with the potential to be exported via this pathway.

scholarly journals Furin-Mediated Cleavage of the Feline Foamy Virus Env Leader Protein

2004 ◽  
Vol 78 (24) ◽  
pp. 13573-13581 ◽  
Author(s):  
Verena Geiselhart ◽  
Patrizia Bastone ◽  
Tore Kempf ◽  
Martina Schnölzer ◽  
Martin Löchelt
Keyword(s):  
Cleavage Site ◽  
Transmembrane Protein ◽  
Foamy Virus ◽  
Proteolytic Processing ◽  
Signal Peptidase ◽  
Amino Acid Residues ◽  
Furin Cleavage ◽  
Furin Cleavage Site ◽  
Leader Protein ◽  
Distinguishing Features

ABSTRACT The molecular biology of spuma or foamy retroviruses is different from that of the other members of the Retroviridae. Among the distinguishing features, the N-terminal domain of the foamy virus Env glycoprotein, the 16-kDa Env leader protein Elp, is a component of released, infectious virions and is required for particle budding. The transmembrane protein Elp specifically interacts with N-terminal Gag sequences during morphogenesis. In this study, we investigate the mechanism of Elp release from the Env precursor protein. By a combination of genetic, biochemical, and biophysical methods, we show that the feline foamy virus (FFV) Elp is released by a cellular furin-like protease, most likely furin itself, generating an Elp protein consisting of 127 amino acid residues. The cleavage site fully conforms to the rules for an optimal furin site. Proteolytic processing at the furin cleavage site is required for full infectivity of FFV. However, utilization of other furin proteases and/or cleavage at a suboptimal signal peptidase cleavage site can partially rescue virus viability. In addition, we show that FFV Elp carries an N-linked oligosaccharide that is not conserved among the known foamy viruses.

scholarly journals Identification of Two myo-Inositol Transporter Genes of Bacillus subtilis

2002 ◽  
Vol 184 (4) ◽  
pp. 983-991 ◽  
Author(s):  
Ken-Ichi Yoshida ◽  
Yoshiyuki Yamamoto ◽  
Kaoru Omae ◽  
Mami Yamamoto ◽  
Yasutaro Fujita
Keyword(s):  
Bacillus Subtilis ◽  
Promoter Region ◽  
Genome Project ◽  
Growth Defect ◽  
Promoter Regions ◽  
Significant Similarity ◽  
Sugar Transporters ◽  
Dnase I Footprinting ◽  
Inositol Uptake

ABSTRACT Among hundreds of mutants constructed systematically by the Japanese groups participating in the functional analysis of the Bacillus subtilis genome project, we found that a mutant with inactivation of iolT (ydjK) exhibited a growth defect on myo-inositol as the sole carbon source. The putative product of iolT exhibits significant similarity with many bacterial sugar transporters in the databases. In B. subtilis, the iolABCDEFGHIJ and iolRS operons are known to be involved in inositol utilization, and its transcription is regulated by the IolR repressor and induced by inositol. Among the iol genes, iolF was predicted to encode an inositol transporter. Inactivation of iolF alone did not cause such an obvious growth defect on inositol as the iolT inactivation, while simultaneous inactivation of the two genes led to a more severe defect than the single iolT inactivation. Determination of inositol uptake by the mutants revealed that iolT inactivation almost completely abolished uptake, but uptake by IolF itself was slightly detectable. These results, as well as the Km and V max values for the IolT and IolF inositol transporters, indicated that iolT and iolF encode major and minor inositol transporters, respectively. Northern and primer extension analyses of iolT transcription revealed that the gene is monocistronically transcribed from a promoter likely recognized by ςsgr;A RNA polymerase and negatively regulated by IolR as well. The interaction between IolR and the iolT promoter region was analyzed by means of gel retardation and DNase I footprinting experiments, it being suggested that the mode of interaction is quite similar to that found for the promoter regions of the iol divergon.

Sign in / Sign up

Export Citation Format

Share Document