Molecular cloning of the GTP‐cyclohydrolase structural gene <i>RIB1</i> of <i>Pichia guilliermondii</i> involved in riboflavin biosynthesis

Liauta-Teglivets, O. Ye.; Hasslacher, Meinhard; Boretskiĭ, Iu R; Kohlwein, Sepp D.; Shavlovskiĭ, G M

doi:10.1002/yea.320111005

Cited by 17 publications

(6 citation statements)

References 26 publications

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“…Finally, methods of classical genetics for analyzing dominance-recessiveness and meiotic segregation have been developed for P. guilliermondii, while methods of molecular genetics have been developed for both organisms (Table 1) (1,40,41,436,437,441,448,454,511). Structural genes of RF biosynthesis have been cloned from these organisms (90,266,277,510,546). A promoter assay system has been developed for C. famata, and several strong promoters have been cloned (194).…”

Section: Transcriptional Regulation In Flavinogenic Yeasts By Ironmentioning

confidence: 99%

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

Abbas

Sibirny

2011

Microbiol Mol Biol Rev

316

272

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SUMMARY Riboflavin [7,8-dimethyl-10-(1′- d -ribityl)isoalloxazine, vitamin B 2 ] is an obligatory component of human and animal diets, as it serves as the precursor of flavin coenzymes, flavin mononucleotide, and flavin adenine dinucleotide, which are involved in oxidative metabolism and other processes. Commercially produced riboflavin is used in agriculture, medicine, and the food industry. Riboflavin synthesis starts from GTP and ribulose-5-phosphate and proceeds through pyrimidine and pteridine intermediates. Flavin nucleotides are synthesized in two consecutive reactions from riboflavin. Some microorganisms and all animal cells are capable of riboflavin uptake, whereas many microorganisms have distinct systems for riboflavin excretion to the medium. Regulation of riboflavin synthesis in bacteria occurs by repression at the transcriptional level by flavin mononucleotide, which binds to nascent noncoding mRNA and blocks further transcription (named the riboswitch). In flavinogenic molds, riboflavin overproduction starts at the stationary phase and is accompanied by derepression of enzymes involved in riboflavin synthesis, sporulation, and mycelial lysis. In flavinogenic yeasts, transcriptional repression of riboflavin synthesis is exerted by iron ions and not by flavins. The putative transcription factor encoded by SEF1 is somehow involved in this regulation. Most commercial riboflavin is currently produced or was produced earlier by microbial synthesis using special selected strains of Bacillus subtilis , Ashbya gossypii , and Candida famata . Whereas earlier RF overproducers were isolated by classical selection, current producers of riboflavin and flavin nucleotides have been developed using modern approaches of metabolic engineering that involve overexpression of structural and regulatory genes of the RF biosynthetic pathway as well as genes involved in the overproduction of the purine precursor of riboflavin, GTP.

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Section: Transcriptional Regulation In Flavinogenic Yeasts By Ironmentioning

confidence: 99%

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

Abbas

Sibirny

2011

Microbiol Mol Biol Rev

316

272

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“…This product represents the first specific precursor for synthesis of riboflavin which requires, in E. coli, the function of various further enzymes [24]. The gene encoding GCH II has been detected in various gram-positive and gram-negative bacteria including E. coli [47], Haemophilus influenzae [23], Azospirillum brasilense [58], Actinobacillus pleuropneumoniae [25], Photobacterium phosphoreum [37], Bacillus subtilis [31,43], and in eukaryotes such as the yeast Saccharomyces cerevisiae [52], the fungus Pichia guillermondii [38], and the plant Arabidopsis thaliana [32]. The organization of genes encoding enzymes of the riboflavin biosynthetic pathway varies among different bacterial species.…”

Section: Introductionmentioning

confidence: 99%

Hemolytic properties and riboflavin synthesis of Helicobacter pylori: cloning and functional characterization of the rib A gene encoding GTP-cyclohydrolase II that confers hemolytic activity to Escherichia coli

Bereswill

Fassbinder

Völzing

et al. 1998

Medical Microbiology and Immunology

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Various strains of Helicobacter pylori were able to lyse erythrocytes from sheep, horse, and human when grown on blood agar. The hemolysis did not depend on the production of the vacuolating cytotoxin VacA as demonstrated by the hemolytic behavior of an isogenic vacA-negative mutant strain. The hemolytic activity could be detected in cell-free supernatants and was not regulated by iron. To isolate genes coding for proteins involved in the destruction of erythrocytes, a plasmid-based DNA library was screened for expression of lytic activity on blood agar. This approach revealed that the H. pylori ribA gene confers hemolytic properties to Escherichia coli. The ribA gene encodes the enzyme GTP-cyclohydrolase II [EC 3.5.4.25] that catalyzes the initial step in the synthesis of riboflavin. The predicted amino acid sequence of the H. pylori RibA protein showed a high degree of similarity to equivalent enzymes from microorganisms and from plants. The single gene on a plasmid restored riboflavin synthesis in a ribA mutant of E. coli and induced hemolytic activity. Furthermore, ribA overexpression was associated with the production of a fluorescent yellow molecule that was not identical with riboflavin. Hemolysis was also seen for the ribA gene from E. coli, indicating that this feature was not specific for the H. pylori gene. The presence of ribA in various H. pylori strains was confirmed by Southern blot hybridization and by polymerase chain reaction with specific primers. This analysis revealed that microdiversity exists within the DNA region upstream from ribA, which was further confirmed by nucleotide sequence analysis.

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“…GCH II functions as a homodimer in E. coli (Richter et al 1993) and a tetramer in Pichia guilliermondii (Teglivets et al 1995). It is competitively inhibited by pyrophosphate (K I 24 AE 7 mM) (Ritz et al 2001).…”

Section: Introductionmentioning

confidence: 98%

Molecular and structural characterization of GTP-cyclohydrolase II in Eremothecium ashbyi NRRL Y-1363: cDNA cloning, comparative sequence analysis and molecular modeling

Sengupta

Chandra

2010

Fungal Biology

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Molecular cloning of the GTP‐cyclohydrolase structural gene RIB1 of Pichia guilliermondii involved in riboflavin biosynthesis

Cited by 17 publications

References 26 publications

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

Hemolytic properties and riboflavin synthesis of Helicobacter pylori: cloning and functional characterization of the rib A gene encoding GTP-cyclohydrolase II that confers hemolytic activity to Escherichia coli

Molecular and structural characterization of GTP-cyclohydrolase II in Eremothecium ashbyi NRRL Y-1363: cDNA cloning, comparative sequence analysis and molecular modeling

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