Interactions of Micromolar Concentrations of Fluoride with Streptococcus rattus FA-1

1990 ◽  
Vol 24 (3) ◽  
pp. 189-197 ◽  
Author(s):  
N. Psarros ◽  
U. Feige ◽  
H. Duschner
Keyword(s):  
Streptococcus Rattus

Glycerol incorporation in certain oral streptococci

1980 ◽  
Vol 30 (3) ◽  
pp. 759-765
Author(s):  
T A Kral ◽  
L Daneo-Moore
Keyword(s):  
Dry Weight ◽  
Defined Medium ◽  
Oral Streptococci ◽  
Chemically Defined Medium ◽  
Low Concentrations ◽  
Saturation Kinetics ◽  
Wild Rats ◽  
Different Strains ◽  
Streptococcus Rattus ◽  
Type Strains

Cells of 30 different strains of oral streptococci were grown in a chemically defined medium supplemented with [14C]glycerol to determine their ability to incorporate the labeled glycerol. Of the five species tested, only two, the rat-type strains (Streptococcus rattus) and strains isolated from wild rats (Streptococcus ferus), were able to incorporate the nonfermentable substrate, glycerol. For those strains capable of incorporating glycerol, the amount incorporated ranged from 0.15 to 0.43% of the cellular dry weight and followed simple saturation kinetics. The amount of glycerol incorporated depended solely on the concentration of glycerol in the growth medium. As a result, cultures exposed to low concentrations of glycerol ceased incorporation of the labeled glycerol before cessation of exponential growth.

scholarly journals Characterization of the Arginine Deiminase Operon of Streptococcus rattus FA-1

2004 ◽  
Vol 70 (3) ◽  
pp. 1321-1327 ◽  
Author(s):  
Ann Griswold ◽  
Yi-Ywan M. Chen ◽  
Jennifer A. Snyder ◽  
Robert A. Burne
Keyword(s):  
Transcriptional Start Site ◽  
Regulatory Protein ◽  
Arginine Deiminase ◽  
Mutans Streptococci ◽  
Ph Homeostasis ◽  
Atp Production ◽  
Dna Libraries ◽  
Genes Encoding ◽  
Streptococcus Rattus

ABSTRACT The arginine deiminase system (ADS) is of critical importance in oral biofilm pH homeostasis and microbial ecology. The ADS consists of three enzymes. Arginine is hydrolyzed by AD (ArcA) to generate citrulline and ammonia. Citrulline is then converted to ornithine and carbamoylphosphate via ornithine carbamoyltransferase (ArcB). Finally, carbamate kinase (ArcC) transfers a phosphate from carbamoylphosphate to ADP, yielding ATP. Ammonia production from this pathway protects bacteria from lethal acidification, and ATP production provides a source of energy for the cells. The purpose of this study was to initiate a characterization of the arc operon of Streptococcus rattus, the least cariogenic and sole ADS-positive member of the mutans streptococci. Using an arcB gene fragment obtained by degenerate PCRs, the FA-1 arc operon was identified in subgenomic DNA libraries and sequence analysis was performed. Results showed that the genes encoding the AD pathway in S. rattus FA-1 are organized as an arcABCDT-adiR operon gene cluster, including the enzymes of the pathway, an arginine-ornithine antiporter (ArcD) and a putative regulatory protein (AdiR). The arcA transcriptional start site was identified by primer extension, and a σ70-like promoter was mapped 5′ to arcA. Reverse transcriptase PCR was used to establish that arcABCDT could be cotranscribed. Reporter gene fusions and AD assays demonstrated that the operon is regulated by substrate induction and catabolite repression, the latter apparently through a CcpA-dependent pathway.

Type-Specific Antigen of Streptococcus rattus Strains (KAY1 and FA1). I. Characterization

1989 ◽  
Vol 271 (1) ◽  
pp. 36-45 ◽  
Author(s):  
Fusao Ota ◽  
Hideaki Nagamune ◽  
Yasuyuki Akiyama ◽  
Hirohisa Kato ◽  
Yasuhiko Yasuoka ◽  
...  
Keyword(s):  
Specific Antigen ◽  
Streptococcus Rattus

Immunochemical analysis and localisation of a cell wall antigen of Streptococcus rattus with a specific monoclonal antibody

1995 ◽  
Vol 282 (4) ◽  
pp. 343-352 ◽  
Author(s):  
Fusao Ota ◽  
Hirohisa Kato ◽  
Katsuhiko Hirota ◽  
Susumu Imai ◽  
Hiroyuki Ishikawa ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Wall ◽  
Immunochemical Analysis ◽  
Specific Monoclonal Antibody ◽  
A Cell ◽  
Streptococcus Rattus

Turning on and turning off the arginine deiminase system in oral streptococci

1998 ◽  
Vol 44 (11) ◽  
pp. 1078-1085 ◽  
Author(s):  
Timothy M Curran ◽  
Yousheng Ma ◽  
Glen C Rutherford ◽  
Robert E Marquis
Keyword(s):  
Cell Growth ◽  
Catabolite Repression ◽  
High Capacity ◽  
Arginine Deiminase ◽  
The Other ◽  
Oral Streptococci ◽  
Permeabilized Cells ◽  
Streptococcus Sanguis ◽  
Glass Slides ◽  
Streptococcus Rattus

The arginine deiminase system in oral streptococci is highly regulated. It requires induction and is repressed by catabolites such as glucose or by aeration. A comparative study of regulation of the system in Streptococcus gordonii ATCC 10558, Streptococcus rattus FA-1, and Streptococcus sanguis NCTC 10904 showed an increase in activity of the system in S. sanguis of some 1467-fold associated with induction-derepression of cells previously uninduced-repressed. The activity of the system was assayed in terms of levels of arginine deiminase, the signature enzyme of the system, in permeabilized cells. Increases in enzyme levels associated with induction-derepression were less for the other two organisms, mainly because of less severe repression, especially for S. rattus FA-1, which was the least sensitive to catabolite repression or aeration. Regulation of the arginine deiminase system involving induction and catabolite repression was demonstrated also with monoorganism biofilms composed of cells of S. sanguis adherent to glass slides. Fully uninduced-repressed cells from suspension cultures or biofilms were compromised in their abilities to catabolize arginine to protect themselves against acid damage. However, it was found that the system can be rapidly turned on or turned off, although induction-derepression did appear to require cell growth. Still, the system could respond rapidly to the availability of arginine to reestablish high capacity for alkali production.Key words: arginine deiminase, oral streptococci, induction-derepression, acid damage, biofilms.

Type-specific Antigen of Streptococcus rattus Strains (KAY1, FA1 and BHT)

1989 ◽  
Vol 271 (2) ◽  
pp. 137-145 ◽  
Author(s):  
Fusao Ota ◽  
Yoshihiro Minato ◽  
Sonia Senesi ◽  
Hideaki Nagamune ◽  
Yasuhiko Satomi ◽  
...  
Keyword(s):  
Specific Antigen ◽  
Streptococcus Rattus
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