Molecular Evolution of hisB Genes

@article{Brilli2003MolecularE,
  title={
Molecular Evolution of hisB Genes
},
  author={Matteo Brilli and Renato Fani},
  journal={Journal of Molecular Evolution},
  year={2003},
  volume={58},
  pages={225-237}
}
  • M. Brilli, R. Fani
  • Published 1 February 2004
  • Biology, Medicine
  • Journal of Molecular Evolution
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… Expand
The origin and evolution of eucaryal HIS7 genes: from metabolon to bifunctional proteins?
TLDR
A comparative analysis of the amino acid sequence of all the available HisH, HisF and HIS7 proteins allowed depicting a likely evolutionary pathway leading to the present-day bifunctional HIS7 genes. Expand
The role of gene fusions in the evolution of metabolic pathways: the histidine biosynthesis case
TLDR
Gene duplication is the most widely known mechanism responsible for the origin and evolution of metabolic pathways; however, several other mechanisms might concur in the process of pathway assembly and gene fusion appeared to be one of the most important and common. Expand
The Evolution of Histidine Biosynthesis in Archaea: Insights into the his Genes Structure and Organization in LUCA
TLDR
It is shown that, in most Archaea, his genes are monofunctional and scattered throughout the genome, suggesting that his operons might have been assembled multiple times during evolution and that in some cases they are the result of recent evolutionary events. Expand
Structural Snapshots of Escherichia coli Histidinol Phosphate Phosphatase along the Reaction Pathway*
TLDR
A catalytic mechanism is proposed requiring the presence of the second metal ion not found in the active sites of previously characterized HAD enzymes, to complete the second half-reaction, reminiscent of two-Mg2+ ion catalysis utilized by DNA and RNA polymerases and many nucleases. Expand
Structural, evolutionary and genetic analysis of the histidine biosynthetic "core" in the genus Burkholderia.
TLDR
Findings are in agreement with the fact that the entire Burkholderiahis operon is heterogeneous, in that it contains "alien" genes apparently not involved in histidine biosynthesis and support the idea that the proteobacterial his operon was piece-wisely assembled. Expand
Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond
TLDR
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. Expand
The Histidinol Phosphate Phosphatase Involved in Histidine Biosynthetic Pathway Is Encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2)
TLDR
Results show that S. coelicolorSCO5208, recently renamed hisN, is the HolPase involved in histidine biosynthesis. Expand
The Origin and Evolution of Operons: The Piecewise Building of the Proteobacterial Histidine Operon
TLDR
A “piecewise” model is proposed for the origin and evolution of proteobacterial his operons, according to which the initially scattered his genes of the ancestor of proteOBacteria coded for monofunctional enzymes and underwent a stepwise compacting process that reached its culmination in some γ-proteobacteria. Expand
On the origin and evolution of biosynthetic pathways: integrating microarray data with structure and organization of the Common Pathway genes
TLDR
A model to explain the evolution of ask and hom genes in proteobacteria is depicted according to which the fused genes are the outcome of a cascade of gene duplication and fusion events that can be traced in the ancestor of γ-proteobacteria. Expand
Molecular evolution of acetohydroxyacid synthase in bacteria
TLDR
The results show the biological significance of AHAS, help to understand the functions of various AHASs in bacteria, and would be useful for developing industrial production strains of branched chain amino acids or novel antimicrobials. Expand
...
1
2
3
4
...

References

SHOWING 1-10 OF 76 REFERENCES
Molecular evolution of the histidine biosynthetic pathway
TLDR
Evidence that the hisA and the hisF genes and their homologues are the result of two successive duplication events that apparently took place before the separation of the three cellular lineages is extended supports the idea that during the early stages of metabolic evolution at least parts of the histidine biosynthetic pathway were mediated by enzymes of broader substrate specificities. Expand
Evolution of the Structure and Chromosomal Distribution of Histidine Biosynthetic Genes
TLDR
The available evidence supports the hypothesis that histidine biosynthesis was assembled by a gene recruitment process and suggests that it is a highly conserved pathway that was probably already present in the last common ancestor of all extant life. Expand
Directed evolution of a ( ba ) 8-barrel enzyme to catalyze related reactions in two different metabolic pathways
Enzymes participating in different metabolic pathways often have similar catalytic mechanisms and structures, suggesting their evolution from a common ancestral precursor enzyme. We sought to createExpand
Histidinol Phosphate Phosphatase, Catalyzing the Penultimate Step of the Histidine Biosynthesis Pathway, Is Encoded byytvP (hisJ) in Bacillus subtilis
TLDR
Observations demonstrated that HolPase is encoded by ytvP in B. subtilis and led to the rename this gene hisJ, a family of related enzymes that are not homologous to the HolPases of Escherichia coli, Salmonella typhimurium, and Haemophilus influenzae. Expand
Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.
TLDR
Findings suggest that HisA and TrpF may have evolved from an ancestral enzyme of broader substrate specificity and underscore that (betaalpha)(8)-barrel enzymes are very suitable for the design of new catalytic activities. Expand
Cloning and characterization of histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2).
TLDR
To investigate the structural organization and the regulation of these genes, genomic libraries from S. coelicolor A3(2) in pUC vectors are constructed and five ORFs which showed significant homology with the his gene products of E. coli are identified. Expand
Cloning of histidine genes of Azospirillum brasilense: Organization of the ABFH gene cluster and nucleotide sequence of the hisB gene
SummaryA cluster of four Azospirillum brasilense histidine biosynthetic genes, hisA, hisB, hisF and hisH, was identified on a 4.5 kb DNA fragment and its organization studied by complementationExpand
Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2).
TLDR
To investigate the structural organization and the regulation of these genes, genomic libraries from S. coelicolor A3(2) in pUC vectors are constructed and five ORFs which showed significant homology with the his gene products of E. coli are identified. Expand
Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): structural similarity to mammalian ALDHs and a plant BADH.
TLDR
The conservation between E. coli BADH and the ALDHs was also evident in the predicted secondary structures and hydrophilicity profiles of the polypeptides, suggesting a similarity in the overall folding patterns of ALDH and BADH, preceding prokaryote-eukaryote divergence. Expand
Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes.
TLDR
It is reported here that rice plants possess the ability to take up exogenously added betaine aldehyde through the roots and convert it to glycinebetaine, resulting in an enhanced salt-tolerance of the plants. Expand
...
1
2
3
4
5
...