PMID:15042344
| Citation |
Brilli, M and Fani, R (2004) Molecular evolution of hisB genes. J. Mol. Evol. 58:225-37 |
|---|---|
| Abstract |
The sixth and eighth steps of histidine biosynthesis are catalyzed by an imidazole glycerol-phosphate (IGP) dehydratase (EC 4.2.1.19) and by a histidinol-phosphate (HOL-P) phosphatase (EC 3.1.3.15), respectively. In the enterobacteria, in Campylobacter jejuni and in Xylella/Xanthomonas the two activities are associated with a single bifunctional polypeptide encoded by hisB. On the other hand, in Archaea, Eucarya, and most Bacteria the two activities are encoded by two separate genes. In this work we report a comparative analysis of the amino acid sequence of all the available HisB proteins, which allowed us to depict a likely evolutionary pathway leading to the present-day bifunctional hisB gene. According to the model that we propose, the bifunctional hisB gene is the result of a fusion event between two independent cistrons joined by domain-shuffling. The fusion event occurred recently in evolution, very likely in the proteobacterial lineage after the separation of the gamma- and the beta-subdivisions. Data obtained in this work established that a paralogous duplication event of an ancestral DDDD phosphatase encoding gene originated both the HOL-P phosphatase moiety of the E. coli hisB gene and the gmhB gene coding for a DDDD phosphatase, which is involved in the biosynthesis of a precursor of the inner core of the outer membrane lipopolysaccharides (LPS). |
| Links |
PubMed Online version:10.1007/s00239-003-2547-x |
| Keywords |
Amino Acid Sequence; Bacteria/genetics; Cluster Analysis; Databases, Genetic; Evolution, Molecular; Gene Duplication; Histidine/genetics; Hydro-Lyases/genetics; Models, Genetic; Phylogeny; Protein Structure, Tertiary; RNA, Ribosomal, 16S/genetics; Sequence Alignment |
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