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CysQ of Cryptosporidium parvum, a Protozoa, May Have Been Acquired from Bacteria by Horizontal Gene Transfer.

Lee JY, Kim S - Genomics Inform (2012)

Bottom Line: Analysis with NCBI's Conserved Domain Tree showed phylogenetic incongruence, in that C. parvum CysQ protein was located within a branch of proteobacteria in the cd01638 domain, a bacterial member of the inositol monophosphatase family.According to Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, the sulfate assimilation pathway, where CysQ plays an important role, is well conserved in most eukaryotes as well as prokaryotes.Therefore, we conclude that C. parvum regained cysQ from proteobacteria by HGT, although its functional role is elusive.

View Article: PubMed Central - PubMed

Affiliation: Department of Bioinformatics & Life Sciences, Soongsil University, Seoul 156-743, Korea.

ABSTRACT
Horizontal gene transfer (HGT) is the movement of genetic material between kingdoms and is considered to play a positive role in adaptation. Cryptosporidium parvum is a parasitic protozoan that causes an infectious disease. Its genome sequencing reported 14 bacteria-like proteins in the nuclear genome. Among them, cgd2_1810, which has been annotated as CysQ, a sulfite synthesis pathway protein, is listed as one of the candidates of genes horizontally transferred from bacterial origin. In this report, we examined this issue using phylogenetic analysis. Our BLAST search showed that C. parvum CysQ protein had the highest similarity with that of proteobacteria. Analysis with NCBI's Conserved Domain Tree showed phylogenetic incongruence, in that C. parvum CysQ protein was located within a branch of proteobacteria in the cd01638 domain, a bacterial member of the inositol monophosphatase family. According to Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, the sulfate assimilation pathway, where CysQ plays an important role, is well conserved in most eukaryotes as well as prokaryotes. However, the Apicomplexa, including C. parvum, largely lack orthologous genes of the pathway, suggesting its loss in those protozoan lineages. Therefore, we conclude that C. parvum regained cysQ from proteobacteria by HGT, although its functional role is elusive.

No MeSH data available.


Related in: MedlinePlus

A simplified sulfate assimilation pathway. Inorganic sulfate is converted to adenosine 5'-phosphosulfate (APS) by ATP sulfurylase (EC 2.7.7.4 and/or EC 2.7.7.5, Class I). APS is phosphorylated by APS kinase (EC 2.7.1.25, Class II) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). PAPS is either transferred to 3'-phosphoadenosine-5'-phosphate (PAP) or reconverted to APS by 3'-phosphoadenosine-5'-phosphatase (EC 3.1.3.7, Class III).
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Figure 2: A simplified sulfate assimilation pathway. Inorganic sulfate is converted to adenosine 5'-phosphosulfate (APS) by ATP sulfurylase (EC 2.7.7.4 and/or EC 2.7.7.5, Class I). APS is phosphorylated by APS kinase (EC 2.7.1.25, Class II) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). PAPS is either transferred to 3'-phosphoadenosine-5'-phosphate (PAP) or reconverted to APS by 3'-phosphoadenosine-5'-phosphatase (EC 3.1.3.7, Class III).

Mentions: CysQ protein participates in sulfate assimilation on sulfur metabolism. In Fig. 2, we show a simplified version of the KEGG pathway, classifying the enzymes into three groups, according to their direction and steps: Class I for EC 2.7.7.4 (CysN) and EC 2.7.7.5 (CysD); Class II for EC 2.7.1.25 (CysC); and Class III for EC 3.1.3.7 (CysQ). If CysQ of C. parvum is a true CysQ enzyme, playing a role in sulfate assimilation in the parasite, the other components of the pathway should be present in it. On the contrary, we could not identify such genes in the annotated gene list.


CysQ of Cryptosporidium parvum, a Protozoa, May Have Been Acquired from Bacteria by Horizontal Gene Transfer.

Lee JY, Kim S - Genomics Inform (2012)

A simplified sulfate assimilation pathway. Inorganic sulfate is converted to adenosine 5'-phosphosulfate (APS) by ATP sulfurylase (EC 2.7.7.4 and/or EC 2.7.7.5, Class I). APS is phosphorylated by APS kinase (EC 2.7.1.25, Class II) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). PAPS is either transferred to 3'-phosphoadenosine-5'-phosphate (PAP) or reconverted to APS by 3'-phosphoadenosine-5'-phosphatase (EC 3.1.3.7, Class III).
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3475487&req=5

Figure 2: A simplified sulfate assimilation pathway. Inorganic sulfate is converted to adenosine 5'-phosphosulfate (APS) by ATP sulfurylase (EC 2.7.7.4 and/or EC 2.7.7.5, Class I). APS is phosphorylated by APS kinase (EC 2.7.1.25, Class II) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). PAPS is either transferred to 3'-phosphoadenosine-5'-phosphate (PAP) or reconverted to APS by 3'-phosphoadenosine-5'-phosphatase (EC 3.1.3.7, Class III).
Mentions: CysQ protein participates in sulfate assimilation on sulfur metabolism. In Fig. 2, we show a simplified version of the KEGG pathway, classifying the enzymes into three groups, according to their direction and steps: Class I for EC 2.7.7.4 (CysN) and EC 2.7.7.5 (CysD); Class II for EC 2.7.1.25 (CysC); and Class III for EC 3.1.3.7 (CysQ). If CysQ of C. parvum is a true CysQ enzyme, playing a role in sulfate assimilation in the parasite, the other components of the pathway should be present in it. On the contrary, we could not identify such genes in the annotated gene list.

Bottom Line: Analysis with NCBI's Conserved Domain Tree showed phylogenetic incongruence, in that C. parvum CysQ protein was located within a branch of proteobacteria in the cd01638 domain, a bacterial member of the inositol monophosphatase family.According to Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, the sulfate assimilation pathway, where CysQ plays an important role, is well conserved in most eukaryotes as well as prokaryotes.Therefore, we conclude that C. parvum regained cysQ from proteobacteria by HGT, although its functional role is elusive.

View Article: PubMed Central - PubMed

Affiliation: Department of Bioinformatics & Life Sciences, Soongsil University, Seoul 156-743, Korea.

ABSTRACT
Horizontal gene transfer (HGT) is the movement of genetic material between kingdoms and is considered to play a positive role in adaptation. Cryptosporidium parvum is a parasitic protozoan that causes an infectious disease. Its genome sequencing reported 14 bacteria-like proteins in the nuclear genome. Among them, cgd2_1810, which has been annotated as CysQ, a sulfite synthesis pathway protein, is listed as one of the candidates of genes horizontally transferred from bacterial origin. In this report, we examined this issue using phylogenetic analysis. Our BLAST search showed that C. parvum CysQ protein had the highest similarity with that of proteobacteria. Analysis with NCBI's Conserved Domain Tree showed phylogenetic incongruence, in that C. parvum CysQ protein was located within a branch of proteobacteria in the cd01638 domain, a bacterial member of the inositol monophosphatase family. According to Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, the sulfate assimilation pathway, where CysQ plays an important role, is well conserved in most eukaryotes as well as prokaryotes. However, the Apicomplexa, including C. parvum, largely lack orthologous genes of the pathway, suggesting its loss in those protozoan lineages. Therefore, we conclude that C. parvum regained cysQ from proteobacteria by HGT, although its functional role is elusive.

No MeSH data available.


Related in: MedlinePlus