Distribution of bacteria with the arylsulfate sulfotransferase activity

1998 ◽  
Vol 21 (4) ◽  
pp. 475-477 ◽  
Author(s):  
Moon-Chang Baek ◽  
Ae-Ran Kwon ◽  
Young-Ja Chung ◽  
Byong-Kak Kim ◽  
Eung-Chil Choi
Keyword(s):  
Arylsulfate Sulfotransferase

scholarly journals Bacterial Arylsulfate Sulfotransferase as a Reporter System

2001 ◽  
Vol 45 (10) ◽  
pp. 673-678 ◽  
Author(s):  
Hee-Jeong Yun ◽  
Ae-Ran Kwon ◽  
Eung-Chil Choi
Keyword(s):  
Reporter System ◽  
Arylsulfate Sulfotransferase

scholarly journals Cloning and Sequencing of theKlebsiellaK-36astAGene, Encoding an Arylsulfate Sulfotransferase

1996 ◽  
Vol 40 (8) ◽  
pp. 531-537 ◽  
Author(s):  
Moon-Chang Baek ◽  
Sook-Kyung Kim ◽  
Dong-Hyun Kim ◽  
Byong-Kak Kim ◽  
Eung-Chil Choi
Keyword(s):  
Cloning And Sequencing ◽  
Arylsulfate Sulfotransferase

Sulfation of Various Alcoholic Groups by an Arylsulfate Sulfotransferase fromDesulfitobacterium hafnienseand Synthesis of Estradiol Sulfate

2012 ◽  
Vol 354 (18) ◽  
pp. 3501-3508 ◽  
Author(s):  
Michael A. van der Horst ◽  
Johan F. T. van Lieshout ◽  
Aleksandra Bury ◽  
Aloysius F. Hartog ◽  
Ron Wever
Keyword(s):  
Arylsulfate Sulfotransferase

scholarly journals Characterization of Two Homologous Disulfide Bond Systems Involved in Virulence Factor Biogenesis in Uropathogenic Escherichia coli CFT073

2009 ◽  
Vol 191 (12) ◽  
pp. 3901-3908 ◽  
Author(s):  
Makrina Totsika ◽  
Begoña Heras ◽  
Daniël J. Wurpel ◽  
Mark A. Schembri
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Infection Model ◽  
Multicopy Plasmid ◽  
Unfolded Proteins ◽  
Upec Strain ◽  
Arylsulfate Sulfotransferase ◽  
Redox Active ◽  
Strain Cft073

ABSTRACT Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the proper folding and functioning of secreted and membrane-associated bacterial proteins. Uropathogenic Escherichia coli (UPEC) strains possess two paralogous disulfide bond systems: the well-characterized DsbAB system and the recently described DsbLI system. In the DsbAB system, the highly oxidizing DsbA protein introduces disulfide bonds into unfolded polypeptides by donating its redox-active disulfide and is in turn reoxidized by DsbB. DsbA has broad substrate specificity and reacts readily with reduced unfolded proteins entering the periplasm. The DsbLI system also comprises a functional redox pair; however, DsbL catalyzes the specific oxidative folding of the large periplasmic enzyme arylsulfate sulfotransferase (ASST). In this study, we characterized the DsbLI system of the prototypic UPEC strain CFT073 and examined the contributions of the DsbAB and DsbLI systems to the production of functional flagella as well as type 1 and P fimbriae. The DsbLI system was able to catalyze disulfide bond formation in several well-defined DsbA targets when provided in trans on a multicopy plasmid. In a mouse urinary tract infection model, the isogenic dsbAB deletion mutant of CFT073 was severely attenuated, while deletion of dsbLI or assT did not affect colonization.

scholarly journals DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium

Microbiology ◽  
2009 ◽  
Vol 155 (12) ◽  
pp. 4014-4024 ◽  
Author(s):  
Dongxia Lin ◽  
Byoungkwan Kim ◽  
James M. Slauch
Keyword(s):  
Disulfide Bond ◽  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Arylsulfate Sulfotransferase ◽  
Type Three Secretion System ◽  
Serovar Typhimurium ◽  
Flagellar Assembly ◽  
Periplasmic Proteins

Disulfide bond formation in periplasmic proteins is catalysed by the DsbA/DsbB system in most Gram-negative bacteria. Salmonella enterica serovar Typhimurium also encodes a paralogous pair of proteins to DsbA and DsbB, DsbL and DsbI, respectively, downstream of a periplasmic arylsulfate sulfotransferase (ASST). We show that DsbL and DsbI function as a redox pair contributing to periplasmic disulfide bond formation and, as such, affect transcription of the Salmonella pathogenicity island 1 (SPI1) type three secretion system genes and activation of the RcsCDB system, as well as ASST activity. In contrast to DsbA/DsbB, however, the DsbL/DsbI system cannot catalyse the disulfide bond formation required for flagellar assembly. Phylogenic analysis suggests that the assT dsbL dsbI genes are ancestral in the Enterobacteriaceae, but have been lost in many lineages. Deletion of assT confers no virulence defect during acute Salmonella infection of mice.

Cloning, sequence analysis, and characterization of theastA gene encoding an Arylsulfate sulfotransferase fromCitrobacter freundii

2001 ◽  
Vol 24 (4) ◽  
pp. 316-322 ◽  
Author(s):  
Jin-Wook Kang ◽  
Yeon-Joo Jeong ◽  
Ae-Ran Kwon ◽  
Hee-Jeong Yun ◽  
Dong-Hyun Kim ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Gene Encoding ◽  
Arylsulfate Sulfotransferase
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