Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from<i>Mus musculus</i>and<i>Homo sapiens</i>

Singh, Nisha; Halliday, Amy C.; Knight, Matthew; Lack, Nathan A.; Lowe, E.D.; Churchill, Grant C.

doi:10.1107/s1744309112035191

Cited by 14 publications

(24 citation statements)

References 18 publications

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“…In Fig. 2A, the positions of the mutant amino acid residues are mapped on the crystal structure of the mouse IMPase 1 homodimer (Protein Data Bank 4AS5) (24). The Thr-95 and Thr-96 residues (Fig.…”

Section: Resultsmentioning

confidence: 99%

Defective Craniofacial Development and Brain Function in a Mouse Model for Depletion of Intracellular Inositol Synthesis

Ohnishi

Murata

Watanabe

et al. 2014

Journal of Biological Chemistry

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Background: Lithium exerts a mood-stabilizing effect and inhibits myo-inositol monophosphatase (IMPase). Results: IMPase mutant mice had impaired jaw formation and mimicked lithium-induced behaviors. Conclusion: Craniofacial development and brain function require intracellular inositol production. Significance: This mouse model reveals molecular mechanisms relevant to understanding lithium's efficacy and inositolmediated developmental processes.

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Section: Resultsmentioning

confidence: 99%

Defective Craniofacial Development and Brain Function in a Mouse Model for Depletion of Intracellular Inositol Synthesis

Ohnishi

Murata

Watanabe

et al. 2014

Journal of Biological Chemistry

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“…S1) (2,23,29,44). Although all amino acids involved in the catalytic mechanism are retained, amino acids associated with substrate binding have mutated in some teleost isoforms.…”

Section: Discussionmentioning

confidence: 99%

“…Two IMPA isoforms (IMPA1 and IMPA2) with different tissue distributions and slightly different enzyme characteristics are present in mammals (37,43). Because of the long-term association of these enzymes with lithium treatments for manic-depressive psychosis there is a wealth of information now available on both isoforms, regarding their chemical structures, tissue distributions, substrate specificities, and physiological functions (2,15,29,44). In direct contrast, very little is known about the structures and functions of IMPA isoforms in lower vertebrates, including teleost fish, other than what can be deduced from the mammalian studies.…”

mentioning

confidence: 99%

Seawater acclimation and inositol monophosphatase isoform expression in the European eel (Anguilla anguilla) and Nile tilapia (Orechromis niloticus)

Kalujnaia

Gellatly

Hazon

et al. 2013

American Journal of Physiology-Regulatory, Integrative and Comp

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Inositol monophosphatase (IMPA) is responsible for the synthesis of inositol, a polyol that can function as an intracellular osmolyte helping re-establish cell volume when exposed to hypertonic environments. Some epithelial tissues in euryhaline teleosts such as the eel and tilapia encounter considerable hyperosmotic challenge when fish move from freshwater (FW) to seawater (SW) environments; however, the roles played by organic osmolytes, such as inositol, have yet to be determined. Syntenic analysis has indicated that, as a result of whole genome- and tandem-duplication events, up to six IMPA isoforms can exist within teleost genomes. Four isoforms are homologs of the mammalian IMPA1 gene, and two isoforms are homologs of the mammalian IMPA2 gene. Although the tissue-dependent isoform expression profiles of the teleost isoforms appear to be species-specific, it was primarily mRNA for the IMPA1.1 isoform that was upregulated in epithelial tissues after fish were transferred to SW (up to 16-fold in eel and 90-fold in tilapia). Although up-regulation of IMPA1.1 expression was evident in many tissues in the eel, more substantial increases in IMPA1.1 expression were found in tilapia tissues, where SW acclimation resulted in up to 2,000-fold increases in protein expression, 16-fold increases in enzyme activity and 15-fold increases in tissue inositol contents. Immunohistochemical studies indicated that the tissue and cellular distribution of IMPA1.1 protein differed slightly between eels and tilapia; however, in both species the basal epithelial cell layers within the skin and fin, and the branchial epithelium and interstitial cells within the kidney, exhibited high levels of IMPA1.1 protein expression.

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“…The tertiary structure of IMPase-like HolPases, as shown using the example of HisN Zm , is very similar to that of various mammalian IMPases (data not shown) including the IMPases of Homo sapiens [29] and Bos taurus [28]. Three Mg 2+ ions have been identified in the active site of these two intensively investigated proteins coordinated by five highly conserved amino acid residues [24, 28, 29].…”

Section: Discussionmentioning

confidence: 80%

“…Three Mg 2+ ions have been identified in the active site of these two intensively investigated proteins coordinated by five highly conserved amino acid residues [24, 28, 29]. These five residues are conserved in HisN Zm , HisN Cg , and all analyzed HisN orthologs.…”

Section: Discussionmentioning

confidence: 99%

Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond

et al. 2017

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Background: The eighth step of L-histidine biosynthesis is carried out by an enzyme called histidinol-phosphate phosphatase (HolPase). Three unrelated HolPase families are known so far. Two of them are well studied: HAD-type HolPases known from Gammaproteobacteria like Escherichia coli or Salmonella enterica and PHP-type HolPases known from yeast and Firmicutes like Bacillus subtilis. However, the third family of HolPases, the inositol monophosphatase (IMPase)-like HolPases, present in Actinobacteria like Corynebacterium glutamicum (HisN) and plants, are poorly characterized. Moreover, there exist several IMPase-like proteins in bacteria (e.g. CysQ, ImpA, and SuhB) which are very similar to HisN but most likely do not participate in L-histidine biosynthesis. Results: Deletion of hisN, the gene encoding the IMPase-like HolPase in C. glutamicum, does not result in complete L-histidine auxotrophy. Out of four hisN homologs present in the genome of C. glutamicum (impA, suhB, cysQ, and cg0911), only cg0911 encodes an enzyme with HolPase activity. The enzymatic properties of HisN and Cg0911 were determined, delivering the first available kinetic data for IMPase-like HolPases. Additionally, we analyzed the amino acid sequences of potential HisN, ImpA, SuhB, CysQ and Cg0911 orthologs from bacteria and identified six conserved sequence motifs for each group of orthologs. Mutational studies confirmed the importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity. Several bacterial proteins containing all identified HolPase motifs, but showing only moderate sequence similarity to HisN from C. glutamicum, were experimentally confirmed as IMPase-like HolPases, demonstrating the value of the identified motifs. Based on the confirmed IMPase-like HolPases two profile Hidden Markov Models (HMMs) were build using an iterative approach. These HMMs allow the fast, reliable detection and differentiation of the two paralog groups from each other and other IMPases. Conclusion: The kinetic data obtained for HisN from C. glutamicum, as an example for an IMPase-like HolPases, shows remarkable differences in enzyme properties as compared to HAD-or PHP-type HolPases. The six sequence motifs and the HMMs presented in this study can be used to reliably differentiate between IMPase-like HolPases and IMPase-like proteins with no such activity, with the potential to enhance current and future genome annotations. A phylogenetic analysis reveals that IMPase-like HolPases are not only present in Actinobacteria and plant but can be found in further bacterial phyla, including, among others, Proteobacteria, Chlorobi and Planctomycetes.

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Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase fromMus musculusandHomo sapiens

Cited by 14 publications

References 18 publications

Defective Craniofacial Development and Brain Function in a Mouse Model for Depletion of Intracellular Inositol Synthesis

Defective Craniofacial Development and Brain Function in a Mouse Model for Depletion of Intracellular Inositol Synthesis

Seawater acclimation and inositol monophosphatase isoform expression in the European eel (Anguilla anguilla) and Nile tilapia (Orechromis niloticus)

Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond

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