Functional characterization of the recombinant human tumour suppressor 101F6 protein, a cytochrome b561 homologue

2012 ◽  
Vol 153 (2) ◽  
pp. 233-242 ◽  
Author(s):  
Mariam C. Recuenco ◽  
Md. Motiur Rahman ◽  
Yoichi Sakamoto ◽  
Fusako Takeuchi ◽  
Hiroshi Hori ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Protein A ◽  
Tumour Suppressor ◽  
Human Tumour ◽  
Cytochrome B561

scholarly journals Human diadenosine triphosphate hydrolase: preliminary characterisation and comparison with the Fhit protein, a human tumour suppressor.

2000 ◽  
Vol 47 (2) ◽  
pp. 435-441 ◽  
Author(s):  
A C Asensio ◽  
C R Rodríguez-Ferrer ◽  
S Oaknin ◽  
P Rotllán
Keyword(s):  
Protein A ◽  
Gel Filtration ◽  
Human Platelets ◽  
Tumour Suppressor ◽  
Human Tumour ◽  
Fhit Protein ◽  
Diadenosine Triphosphate

Human platelets diadenosine triphosphatase was characterised and compared with the Fhit protein, a human tumour suppressor with diadenosine triphosphatase activity. Both enzymes exhibit similar Km, are similarly activated by Mg2+, Ca2+ and Mn2+, and inhibited by Zn2+ and suramin. However, they are differentially inhibited by Fhit antibodies and exhibit differences in gel-filtration behaviour.

Functional expression and characterization of human 101F6 protein, a homologue of cytochrome b561 and a candidate tumor suppressor gene product

BioFactors ◽  
2008 ◽  
Vol 34 (3) ◽  
pp. 219-230 ◽  
Author(s):  
Mariam C. Recuenco ◽  
Masamitsu Fujito ◽  
Yoichi Sakamoto ◽  
Motonari Tsubaki ◽  
M. D. Motiur Rahman ◽  
...  
Keyword(s):  
Tumor Suppressor ◽  
Tumor Suppressor Gene ◽  
Gene Product ◽  
Protein A ◽  
Functional Expression ◽  
Suppressor Gene ◽  
Candidate Tumor Suppressor Gene ◽  
Cytochrome B561 ◽  
Tumor Suppressor Gene Product

scholarly journals Functional Characterization of pGKT2, a 182-Kilobase Plasmid Containing the xplAB Genes, Which Are Involved in the Degradation of Hexahydro-1,3,5-Trinitro-1,3,5-Triazine by Gordonia sp. Strain KTR9

2010 ◽  
Vol 76 (19) ◽  
pp. 6329-6337 ◽  
Author(s):  
Karl J. Indest ◽  
Carina M. Jung ◽  
Hao-Ping Chen ◽  
Dawn Hancock ◽  
Christine Florizone ◽  
...  
Keyword(s):  
Amino Acid Sequence Identity ◽  
Inorganic Nitrogen ◽  
Cytochromes P450 ◽  
Functional Characterization ◽  
Protein A ◽  
Nitrogen Sources ◽  
Pcr Analysis ◽  
Bacterial Cells ◽  
Glutamine Synthase

ABSTRACT Several microorganisms have been isolated that can transform hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), a cyclic nitramine explosive. To better characterize the microbial genes that facilitate this transformation, we sequenced and annotated a 182-kb plasmid, pGKT2, from the RDX-degrading strain Gordonia sp. KTR9. This plasmid carries xplA, encoding a protein sharing up to 99% amino acid sequence identity with characterized RDX-degrading cytochromes P450. Other genes that cluster with xplA are predicted to encode a glutamine synthase-XplB fusion protein, a second cytochrome P450, Cyp151C, and XplR, a GntR-type regulator. Rhodococcus jostii RHA1 expressing xplA from KTR9 degraded RDX but did not utilize RDX as a nitrogen source. Moreover, an Escherichia coli strain producing XplA degraded RDX but a strain producing Cyp151C did not. KTR9 strains cured of pGKT2 did not transform RDX. Physiological studies examining the effects of exogenous nitrogen sources on RDX degradation in strain KTR9 revealed that ammonium, nitrite, and nitrate each inhibited RDX degradation by up to 79%. Quantitative real-time PCR analysis of glnA-xplB, xplA, and xplR showed that transcript levels were 3.7-fold higher during growth on RDX than during growth on ammonium and that this upregulation was repressed in the presence of various inorganic nitrogen sources. Overall, the results indicate that RDX degradation by KTR9 is integrated with central nitrogen metabolism and that the uptake of RDX by bacterial cells does not require a dedicated transporter.

scholarly journals Structural and Functional Characterization of a New Double Variant Haemoglobin (HbG-Philadelphia/Duarte α268Asn→Lysβ262Ala→Pro)

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Antonella Fais ◽  
Mariano Casu ◽  
Paolo Ruggerone ◽  
Matteo Ceccarelli ◽  
Simona Porcu ◽  
...  
Keyword(s):  
Md Simulation ◽  
Tertiary Structure ◽  
Functional Characterization ◽  
Protein A ◽  
Oxygen Affinity ◽  
Functional Study ◽  
Substitution Effects ◽  
Simulation Studies ◽  
First Case

We report the first case of cosegregation of two haemoglobins (Hbs): HbG-Philadelphia [α68(E17)Asn→Lys] and HbDuarte [β62(E6)Ala→Pro]. The proband is a young patient heterozygous also for β∘-thalassaemia. We detected exclusively two haemoglobin variants: HbDuarte and HbG-Philadelphia/Duarte. Functional study of the new double variant HbG-Philadelphia/Duarte exhibited an increase in oxygen affinity, with a slight decrease of cooperativity and Bohr effect. This functional behaviour is attributed to β62Ala→Pro instead of α68Asn→Lys substitution. Indeed, HbG-Philadelphia isolated in our laboratory from blood cells donor carrier for this variant is not affected by any functional modification, whereas purified Hb Duarte showed functional properties very similar to the double variant. NMR and MD simulation studies confirmed that the presence of Pro instead of Ala at the β62 position produces displacement of the E helix and modifications of the tertiary structure. The substitution α68(E17)Asn→Lys does not cause significant structural and dynamical modifications of the protein. A possible structure-based rational of substitution effects is suggested.

Functional characterization of replication protein A2 (RPA2) from Cryptosporidium parvum

Microbiology ◽  
2004 ◽  
Vol 150 (5) ◽  
pp. 1197-1205 ◽  
Author(s):  
Jason J. Millership ◽  
Xiaomin Cai ◽  
Guan Zhu
Keyword(s):  
Dna Binding ◽  
Cryptosporidium Parvum ◽  
Functional Characterization ◽  
Protein A ◽  
Replication Protein ◽  
Start Codon ◽  
Heterologous Proteins ◽  
Single Stranded Dna

Replication protein A (RPA) is a heterotrimeric complex of single-stranded DNA-binding proteins that play multiple roles in eukaryotic DNA metabolism. The RPA complex is typically composed of heterologous proteins (termed RPA1, RPA2 and RPA3) in animals, plants and fungi, which possess different functions. Previously, two distinct, short-type RPA large subunits (CpRPA1 and CpRPA1B) from the apicomplexan parasite Cryptosporidium parvum were characterized. Here are reported the identification and characterization of a putative middle RPA subunit (CpRPA2) from this unicellular organism. Although the CpRPA2 gene encodes a predicted 40·1 kDa peptide, which is larger than other RPA2 subunits characterized to date, Western blot analysis of oocyst preparations detected a native CpRPA2 protein with a molecular mass of approximately 32 kDa, suggesting that CpRPA2 might undergo post-translational cleavage or the gene was translated at an alternative start codon. Immunofluorescence microscopy using a rabbit anti-CpRPA2 antibody revealed that CpRPA2 protein was mainly distributed in the cytosol (rather than the nuclei) of C. parvum sporozoites. Semi-quantitative RT-PCR data indicated that CpRPA2 was differentially expressed in a tissue culture model with highest expression in intracellular parasites infecting HCT-8 cells for 36 and 60 h. Sequence comparison suggests that RPA2 is a group of poorly conserved proteins. Nonetheless, functional analyses of recombinant proteins confirmed that CpRPA2 is a single-stranded DNA-binding protein and that it could serve as an in vitro phosphorylation target by a DNA-dependent protein kinase. The minimal length of poly(dT) required for CpRPA2 binding is 17 nucleotides, and the DNA-binding capability was inhibited by phosphorylation in vitro. These observations provide additional evidence on the divergence of RPA proteins between C. parvum and host, implying that the parasite DNA replication machinery could be explored as a chemotherapeutic target.

Functional characterization of novel tumour suppressor galectin-2 in hepatocellular carcinoma

2016 ◽  
Vol 61 ◽  
pp. S62
Author(s):  
F.C.F. Ko ◽  
K.W. Lee ◽  
W.C.S. Tai ◽  
Z. Leung ◽  
J.W.P. Yam
Keyword(s):  
Hepatocellular Carcinoma ◽  
Functional Characterization ◽  
Tumour Suppressor
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