Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.12.7.2 (hydrogenase)
 3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nickel/cobalt transporters (NiCoTs), a family of secondary metal transporters in prokaryotes and fungi, are characterized by an eight-transmembrane-domain (TMD) architecture and mediate high-affinity uptake of cobalt and/or nickel ions into the cells. One of the strongly conserved regions within the NiCoTs is the signature sequence RHA(V/F)DADHI within TMD II. This stretch of amino acid residues plays an important role in the affinity, velocity and specificity of metal transport. Some relatives of the NiCoTs, named HupE, UreJ and UreH, contain a similar signature sequence and are encoded within or adjacent to [NiFe] hydrogenase or urease operons, or elsewhere in the genome of many prokaryotes. HupE and UreH from Rhodopseudomonas palustris CGA009 and UreJ from Cupriavidus necator H16 were shown to mediate Ni(2+) transport upon heterologous production in E. coli. Other variants of NiCoTs are found in many marine cyanobacteria and in plants. The cyanobacterial proteins are encoded by a segment adjacent to the genes for [Ni] superoxide dismutase and a corresponding putative maturation peptidase. The plant proteins contain N-terminal sequences resembling bipartite transit peptides of thylakoid lumenal and thylakoid integral membrane precursor proteins; expression of a YFP-fusion protein in transfected leaf cells is consistent with targeting of this protein to the plastid, but the function of the plant gene product has yet to be demonstrated.
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PMID:Secondary transporters for nickel and cobalt ions: theme and variations. 1615 32

Entamoeba histolytica is known for its extraordinary capacity to destroy human tissues, leading to invasive diseases such as ulcerative colitis or extra-intestinal abscesses. In order to identify the virulence factors of this parasite phenotypes and proteomes of two recently identified genetically related cell lines (A and B), derived from the laboratory E. histolytica isolate HM-1:IMSS, were compared. Both cell lines are indistinguishable on the basis of highly polymorphic tandem repeat DNA sequences. However, cell line A is incapable to induce liver abscesses in experimentally infected rodents, whereas cell line B provokes considerable abscesses. Phenotypic analyses revealed increased hemolytic activity, lower growth rate, smaller cell size, reduced cysteine peptidase activity and lower resistance to nitric oxide stress for cell line A. In contrast, no differences between the two cell lines were found for cytopathic activity, erythrophagocytosis, digestion of erythrocytes or resistance to complement, hydrogen peroxide and superoxide radical anions. Proteomic comparison by 2-D DIGE followed by MS, identified a total of 21 proteins with higher abundance in cell line A and ten proteins with higher abundance in cell line B. Remarkably, three differentially up-regulated antioxidants were exclusively found in the pathogenic cell line B. Notably, only for two differentially regulated proteins, namely a Fe-hydrogenase and a C2 domain protein, a similar type was found at the level of transcription. Summarized, a defined set of different proteins could be identified between cell lines A and B. These molecules may have an important role in amoeba pathogenicity.
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PMID:Comparison of two genetically related Entamoeba histolytica cell lines derived from the same isolate with different pathogenic properties. 1968 50