The Missing Link in Plant Histidine Biosynthesis: Arabidopsis myoinositol monophosphatase-like2 Encodes a Functional Histidinol-Phosphate Phosphatase

Lindsay N. Petersen; Sandra Marineo; Salvatore Mandalà; Faezah Davids; Bryan T. Sewell; Robert A. Ingle

doi:10.1104/pp.109.150805

The Missing Link in Plant Histidine Biosynthesis: Arabidopsis myoinositol monophosphatase-like2 Encodes a Functional Histidinol-Phosphate Phosphatase

PLANT PHYSIOLOGY ◽

10.1104/pp.109.150805 ◽

2009 ◽

Vol 152 (3) ◽

pp. 1186-1196 ◽

Cited By ~ 28

Author(s):

Lindsay N. Petersen ◽

Sandra Marineo ◽

Salvatore Mandalà ◽

Faezah Davids ◽

Bryan T. Sewell ◽

...

Keyword(s):

Histidine Biosynthesis ◽

Missing Link ◽

Histidinol Phosphate Phosphatase

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PA0335, a Gene Encoding Histidinol Phosphate Phosphatase, Mediates Histidine Auxotrophy in Pseudomonas aeruginosa

Applied and Environmental Microbiology ◽

10.1128/aem.02593-19 ◽

2019 ◽

Vol 86 (5) ◽

Author(s):

Yulu Wang ◽

Liyue Wang ◽

Jian Zhang ◽

Xintong Duan ◽

Yuqi Feng ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Amino Acid ◽

Opportunistic Pathogen ◽

Growth Defect ◽

Histidine Biosynthesis ◽

Common Amino Acid ◽

Content Type ◽

Growth And Survival ◽

Origin And Evolution ◽

Histidinol Phosphate Phosphatase

ABSTRACT The biosynthesis of histidine, a proteinogenic amino acid, has been extensively studied due to its importance in bacterial growth and survival. Histidinol-phosphate phosphatase (Hol-Pase), which is responsible for the penultimate step of histidine biosynthesis, is generally the last enzyme to be characterized in many bacteria because its origin and evolution are more complex compared to other enzymes in histidine biosynthesis. However, none of the enzymes in histidine biosynthesis, including Hol-Pase, have been characterized in Pseudomonas aeruginosa, which is an important opportunistic Gram-negative pathogen that can cause serious human infections. In our previous work, a transposon mutant of P. aeruginosa was found to display a growth defect on glucose-containing minimal solid medium. In this study, we found that the growth defect was due to incomplete histidine auxotrophy caused by PA0335 inactivation. Subsequently, PA0335 was shown to encode Hol-Pase, and its function and enzymatic activity were investigated using genetic and biochemical methods. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in P. aeruginosa were examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) were found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) were essential because deletion of each resulted in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion caused incomplete histidine auxotrophy. Taken together, our results outline the histidine synthesis pathway of P. aeruginosa. IMPORTANCE Histidine is a common amino acid in proteins. Because it plays critical roles in bacterial metabolism, its biosynthetic pathway in many bacteria has been elucidated. However, the pathway remains unclear in Pseudomonas aeruginosa, an important opportunistic pathogen in clinical settings; in particular, there is scant knowledge about histidinol-phosphate phosphatase (Hol-Pase), which has a complex origin and evolution. In this study, P. aeruginosa Hol-Pase was identified and characterized. Furthermore, the roles of all other predicted genes involved in histidine biosynthesis were examined. Our results illustrate the histidine synthesis pathway of P. aeruginosa. The knowledge obtained from this study may help in developing strategies to control P. aeruginosa-related infections. In addition, some enzymes of the histidine synthesis pathway from P. aeruginosa might be used as elements of histidine synthetic biology in other industrial microorganisms.

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Histidinol Phosphate Phosphatase, Catalyzing the Penultimate Step of the Histidine Biosynthesis Pathway, Is Encoded byytvP (hisJ) in Bacillus subtilis

Journal of Bacteriology ◽

10.1128/jb.181.10.3277-3280.1999 ◽

1999 ◽

Vol 181 (10) ◽

pp. 3277-3280 ◽

Cited By ~ 13

Author(s):

Dominique le Coq ◽

Sabine Fillinger ◽

Stéphane Aymerich

Keyword(s):

Escherichia Coli ◽

Saccharomyces Cerevisiae ◽

Bacillus Subtilis ◽

Haemophilus Influenzae ◽

Fusion Protein ◽

Salmonella Typhimurium ◽

Unknown Function ◽

Biosynthesis Pathway ◽

Histidine Biosynthesis ◽

Histidinol Phosphate Phosphatase

ABSTRACT The deduced product of the Bacillus subtilis ytvP gene is similar to that of ORF13, a gene of unknown function in the Lactococcus lactis histidine biosynthesis operon. AB. subtilis ytvP mutant was auxotrophic for histidine. The only enzyme of the histidine biosynthesis pathway that remained uncharacterized in B. subtilis was histidinol phosphate phosphatase (HolPase), catalyzing the penultimate step of this pathway. HolPase activity could not be detected in crude extracts of the ytvP mutant, while purified glutathione S-transferase-YtvP fusion protein exhibited strong HolPase activity. These observations demonstrated that HolPase is encoded by ytvP inB. subtilis and led us to rename this genehisJ. Together with the HolPase of Saccharomyces cerevisiae and the presumed HolPases ofL. lactis and Schizosaccharomyces pombe, HisJ constitutes a family of related enzymes that are not homologous to the HolPases of Escherichia coli, Salmonella typhimurium, and Haemophilus influenzae.

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