Kinetic behaviour of WT 1's zinc finger domain in binding to the alpha-actinin-1 mRNA.

The zinc finger transcription factor Wilms tumour protein (WT 1) is known for its essential involvement in the development of the genitourinary system as well as of other organs and tissues. WT 1 is capable of selectively binding either DNA or mRNA targets. A KTS insertion due to alternative splicing between the zinc fingers 3 and 4 and an unconventional zinc finger 1 are the unique features that distinguish WT 1 from classical DNA-binding C(2)H(2)-type zinc finger proteins.

New insights into DNA-binding behavior of Wilms tumor protein (WT1)--a dual study.

Wilms Tumor suppressor protein (WT1) is a transcription factor that is involved in a variety of developmental functions during organ development. It is also implicated in the pathology of several different cancer forms. The protein contains four C(2)H(2)-type zinc fingers and it specifically binds GC-rich sequences in the promoter regions of its target genes, which are either up or down regulated.

Isolation and expression of UB05, a Plasmodium falciparum antigen recognised by antibodies from semi-immune adults in a high transmission endemic area of the Cameroonian rainforest.

Background: Antibodies in adults living in malaria endemic areas that target specific parasite antigens are implicated in protective immunity to infection and disease. This study aimed to identify, isolate and characterise targets of protective immunity in malaria. A Plasmodium falciparum antigen termed UB05 (Genbank Accession Number DQ235690: PlasmoDB PF10_ 0372) that had been isolated by immunoscreening with semi-immune sera was studied.

Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.

The specific insertion of a divalent metal ion into tetrapyrrole macrocycles is catalyzed by a group of enzymes called chelatases. Distortion of the tetrapyrrole has been proposed to be an important component of the mechanism of metallation. We present the structures of two different inhibitor complexes: (1) N-methylmesoporphyrin (N-MeMP) with the His183Ala variant of Bacillus subtilis ferrochelatase; (2) the wild-type form of the same enzyme with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride (dSDP).