P1-0104 — Final report
1.
First structural and biochemical determination of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis

Cyclic nucleotide monophosphate phosphodiesterase we have crystalised and identified as the Rv0805 gene product is, to date, the only identifiable cNMP PDE in the genome of M. tuberculosis. We have shown that Rv0805 is a cAMP/cGMP dual specificity PDE, and is unrelated in amino acid sequence to the mammalian cNMP PDEs. The structure of the catalytic core of Rv0805 was found distantly related to the calcineurin-like phosphatases, however possessing a unique substrate binding pocket. The enzyme seems be potential target for studying its role in Mtb pathogenesis.

COBISS.SI-ID: 3583770
2.
Microtubule end-anchoring protein ninein dynamics in epithelial cells, microtubular relocation and possible involvement in intercellular communication

Cell-to-cell contact and polarisation of epithelial cells involve a major reorganisation of the microtubules and centrosomal components. We established that ninein is highly dynamic and that, in epithelial cells, it is present not only at the centrosome but also in the cytoplasm as distinct speckles. We found ninein speckles are released, during epithelial differentiation, from the centrosome and move in a microtubule-dependent manner within the cytoplasm and thus establish that epithelial cells possess the mechanical means for relocation of ninein to non-centrosomal anchoring sites.

COBISS.SI-ID: 3794970
3.
Regulation of the lanosterol 14alpha-demethylase (CYP51) gene at the cholesterol homeostasis

This Cover Article is contributing basic knowledge on the regulation of lanosterol 14alpha-demethylase (CYP51) we have cloned previously. The enzyme responds to cholesterol feedback regulation through sterol regulatory element binding proteins (SREBPs). The majority of cAMP-dependent transactivation is mediated through a single CRE (CYP51-CRE2). Exposure of JEG-3 cells to forskolin, a mediator of the cAMP-dependent signaling pathway, provokes an immediate early response of CYP51, which has not been described before for any cholesterogenic gene.

COBISS.SI-ID: 20426969
4.
Naturally occurring phenolic compounds as co-inhibitors of the cloned bezoate para-hydroxylase (BPH): new antifungal drug development

A novel cytochrome P450 was identified in the pathogenic filamentous ascomycete C. lunatus (plant and opportunistic human pathogen). The protein, classified into the CYP53 family, was capable of para-hydroxylation of benzoate. To guide functional analyses, protein structure was predicted by homology modeling. Some naturally occurring antifungal phenolic compounds inhibited CYP53A15, increasingly in the presence of benzoate. The result was exposed in the 21st volume of SciBX (2008) published by BioCentury and Nature, as being interesting for new, alternative antifungal drug development.

COBISS.SI-ID: 3935770
5.
Erythropoetin receptor data base

A combination of a review article on EpoR and elaborated database harbouring a number of links with other gene and protein data basis. Published in the Nature on line edition.

COBISS.SI-ID: 23209945