Academic Journal
BMC Microbiology / Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond
| العنوان: | BMC Microbiology / Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond |
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| المؤلفون: | Kulis-Horn, Robert, Rückert, Christian, Kalinowski, Jörn, Persicke, Marcus |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | HisN Cg0911 Histidinol-phosphate phosphatase (HolPase) Inositol monophosphatase (IMPase)-like Corynebacterium glutamicum Kinetic data Sequence motifs Phylogenetic analysis |
| الوصف: | 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 ... |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1471-2180 |
| Relation: | vignette : https://noah.nrw/titlepage/urn/urn:nbn:de:0070-pub-29131106/128; MEDLINE:28720084; ISI:000405787400001; urn:nbn:de:0070-pub-29131106; https://nbn-resolving.org/urn:nbn:de:0070-pub-29131106; system:bielefeld_pub_2913110 |
| DOI: | 10.1186/s12866-017-1069-4 |
| الاتاحة: | https://nbn-resolving.org/urn:nbn:de:0070-pub-29131106 https://doi.org/10.1186/s12866-017-1069-4 https://noah.nrw/doi/10.1186/s12866-017-1069-4 |
| Rights: | Urheberrechtsschutz |
| رقم الانضمام: | edsbas.9855B979 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 14712180 |
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| DOI: | 10.1186/s12866-017-1069-4 |