The biosynthesis of the histidine-rich protein of Plasmodium lophurae and the cloning of its gene in Escherichia coli

1985 ◽  
Vol 14 (1) ◽  
pp. 1-10 ◽  
Author(s):  
A KILEJIAN ◽  
S CHEN ◽  
A SLOMA
1982 ◽  
Vol 79 (4) ◽  
pp. 1008-1011 ◽  
Author(s):  
J. Schnier ◽  
M. Kimura ◽  
K. Foulaki ◽  
A. R. Subramanian ◽  
K. Isono ◽  
...  

2002 ◽  
Vol 184 (7) ◽  
pp. 1952-1957 ◽  
Author(s):  
Marion Graupner ◽  
Huimin Xu ◽  
Robert H. White

ABSTRACT The Methanococcus jannaschii gene MJ0671 was cloned and overexpressed in Escherichia coli, and its gene product was tested for its ability to catalyze the pyridine nucleotide-dependent reduction of either 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate (compound 3) to 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate (compound 4) or 5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate (compound 7) to 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate (compound 5). Only compound 3 was found to serve as a substrate for the enzyme. NADPH and NADH functioned equally well as the reductants. This specificity for the reduction of compound 3 was also confirmed by using cell extracts of M. jannaschii and Methanosarcina thermophila. Thus, this step in riboflavin biosynthesis in these archaea is the same as that found in yeasts. The absence of the other genes in the biosynthesis of riboflavin in Archaea is discussed.


2008 ◽  
Vol 52 (8) ◽  
pp. 2929-2932 ◽  
Author(s):  
Vincent Cattoir ◽  
Patrice Nordmann ◽  
Jesus Silva-Sanchez ◽  
Paula Espinal ◽  
Laurent Poirel

ABSTRACT A novel QnrB-like plasmid-mediated resistance determinant, QnrB19, was identified from an Escherichia coli clinical isolate from Colombia. Its gene was associated with an ISEcp1-like insertion element that did not act as a promoter for its expression. Using an in vitro model of transposition, we showed that the ISEcp1-like element was able to mobilize the qnrB19 gene.


1987 ◽  
Vol 169 (2) ◽  
pp. 751-757 ◽  
Author(s):  
A Ben-Bassat ◽  
K Bauer ◽  
S Y Chang ◽  
K Myambo ◽  
A Boosman ◽  
...  

Author(s):  
Tanis McMahon ◽  
Jillian Bastian ◽  
Inas Alshawa ◽  
Alexander Gill

Verotoxin-producing Escherichia coli (VTEC; also known as Shiga toxin-producing E. coli ) are a significant cause of foodborne illnesses around the world. Due to the serological and genomic diversity of VTEC, methods of detection for VTEC in food samples require detection of verotoxin or its gene vt (also known as stx ). The current taxonomy of vt identifies three vt1 (a,c,d) and seven vt2 (a to g) subtypes. PCR detection of vt is convenient and rapid, but protocols may not detect all currently identified variants or subtypes of vt . The Health Canada Compendium of Analytical Methods for the analysis of food for VTEC is MFLP-52. MFLP-52 includes a VT Screening PCR that is used to determine the presumptive presence of VTEC by the detection of vt in food enrichments, and to differentiate VTEC from other isolates. The VT Screening PCR was developed prior to the establishment of the current vt taxonomy. An evaluation of VT Screening PCR for detection of the ten established vt -subtypes was performed and it was discovered that the method could not detect subtypes vt1d and vt2f . Additional primers and a modified protocol were developed and the modified VT Screening PCR was tested against an inclusivity panel of 50 VTEC strains, including representatives of ten vt -subtypes, and an exclusivity panel of 30 vt negative E. coli from various sources, to ensure specificity. The reliability of MFLP-52 with the modified VT Screening PCR was assessed by analysis of four priority food matrices (ground beef, lettuce, cheese and apple cider) inoculated with a VTEC strain at 2 to 5 CFU per 25 g. The modified VT Screening PCR was determined to be able to detect all ten vt -subtypes and reliably detect the presence of VTEC in all tested food enrichments.


2003 ◽  
Vol 49 (4) ◽  
pp. 294-300 ◽  
Author(s):  
Joëlle Maréchal ◽  
Renata Santos ◽  
Yasser Hammad ◽  
Nicole Alloisio ◽  
Anne-Marie Domenach ◽  
...  

The Frankia sp. strain ACN14a superoxide dismutase SodF was previously shown to be induced in response to Alnus glutinosa root exudates, and its gene was sequenced. We report here the sequence of the 9-kb genomic segment surrounding the sodF gene and further characterize this gene and its product. Nine ORFs coding for various proteins, such as regulators, acetyl-CoA transferases, and a bacterioferritin A next to the sodF gene, were found. Northern blot analysis showed that the sodF gene was expressed as a major 1-kb transcript, which indicates that it has its own promoter. The sodF gene strongly complemented an Escherichia coli triple mutant (sodA sodB recA), restoring aerobic growth when the gene was expressed from the synthetic tac promoter but when expressed from its own promoter showed only slight rescue, suggesting that it was poorly recognized by the E. coli RNA polymerase. It is noteworthy that this is the first time that a Frankia gene has been reported to complement an E. coli mutant. The superoxide dismutase activity of the protein was inactivated by hydrogen peroxide, indicating that the metal ligand is iron, which is supported by analysis of the protein sequence. Thus, the SodF protein induced in Frankia by root exudates is an iron-containing enzyme similar to the one present in the nodules.Key words: Frankia, iron superoxide dismutase, sodF, E. coli complementation.


2007 ◽  
Vol 51 (11) ◽  
pp. 4009-4014 ◽  
Author(s):  
Delphine Girlich ◽  
Roland Leclercq ◽  
Thierry Naas ◽  
Patrice Nordmann

ABSTRACT A chromosomal β-lactamase gene from Bacillus clausii NR, which is used as a probiotic, was cloned and expressed in Escherichia coli. It encodes a clavulanic acid-susceptible Ambler class A β-lactamase, BCL-1, with a pI of 5.5 and a molecular mass of ca. 32 kDa. It shares 91% and 62% amino acid identity with the chromosomally encoded PenP penicillinases from B. clausii KSM-K16 and Bacillus licheniformis, respectively. The hydrolytic profile of this β-lactamase includes penicillins, narrow-spectrum cephalosporins, and cefpirome. This chromosome-encoded enzyme was inducible in B. clausii, and its gene is likely related to upstream-located regulatory genes that share significant identity with those reported to be upstream of the penicillinase gene of B. licheniformis. The bla BCL-1 gene was located next to the known chromosomal aadD2 gene and the erm34 gene, which encode resistance to aminoglycosides and macrolides, respectively. Similar genes were found in a collection of B. clausii reference strains.


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