II. REVISIÓN DE LA LITERATURA
2.1. Antecedentes
2.2.2. Comprensión Lectora
2.2.2.9. La evaluación de la comprensión lectora: dificultades y
Chapter 5 showed the construction and use of the Hsp90-free strain PP30/10. Here both genomic copies of the Hsp90-encoding genes (HSC82 and HSP82) have been replaced by KanMX4 sequences, with viability being conferred by the URA3 vector YEplac 195-//5CS2. By introducing mutated Hsp90-encoding genes on a secondary plasmid, then counterselecting for the f//M5-containing YEplacl95-7/5C52 vector, the effects of these mutations on Hsp90 production and functionality can be studied. This strain should therefore have many uses in furthering understanding of the exact functions of Hsp82 and Hsc82 their expression and the differences in their degradation. The strain may also prove useful in studying expression and function of the C.albicans Hsp90.
Further experiments are necessary to locate the partial proteolytic signal housed within Hsp82. Figure 4.7 shows that whereas the heat shock protein encoded by HSP82 undergoes stationary phase incomplete degradation, its constitutive cousin Hsc82 does not. Domain swap proteins will help to locate the Hsp82 degron. At the time of writing chimeric proteins are being expressed in PP30/10, these being comprised of either the amino terminus of Hsc82 linked to the C-terminal domain of Hsp82, or the C-terminal domain of Hsc82 with the N-terminus of Hsp82. Expression of these chimeras in an Hsp90 free host should indicate if the partial proteolytic signal of Hsp82 is housed within its amino or carboxyl domains. In the event that both domains are required for partial proteolysis, asymmetric chimeras should be formed. Figures 4.1 and 4.5 have revealed that ubiquitination may play a key role in Hsp82 incomplete degradation. In order to confirm that this proteolysis requires prior ubiquitination it is necessary to prove the existence of ubiquitin-conjugated adducts. This can be achieved by the co-expression of centromeric vectors for HSP82 and myc-tagged ubiquitin, in an Hsp90 free host. The Hsp90 peptides from early logarithmic, late logarithmic and stationary phase cells, can be immunoprecipitated with Hsp90 antisera. These fragments can be separated by SDS-PAGE, western blotted and probed with Anti-myc antibodies. In this way the existence of ubiquitinated Hsp90 adducts can be visualised. Furthermore by comparing the immunoprecipitated ubiquitin conjugated Hsp90 fragments from wild type cells with those obtained from mutants of the ubiquitin-proteolytic pathway, it should be possible to discover the ubiquitination machinery responsible for this conjugation. Figure 4.3 shows that the 90kDa heat shock proteins of both S.cerevisiae and C.albicans cells undergo similar partial breakdowns. It will be interesting to discover if the incomplete degradations of Hsp90 occur by similar mechanisms in both species. The most direct way to study this may be to study the production and degradation of C.albicans Hsp90 in S.cerevisiae ubiquitination system mutants. For example, if C.albicans Hsp90 is expressed in a Sl5 0A h sp 8 2 ::K a n M X 4 ;H S C 8 2 host, all
degradation products should be from the C.albicans protein. The expression of the Candida gene in S.cerevisiae PP30/10, will also show if the Candida protein can confer essential Hsp90 functions in S.cerevisiae, and reveal if the Candida protein undergoes a stationary phase degradation in S.cerevisiae identical to that normally seen in C.albicans. Preliminary results (Fig. 4.3) indicate that these degradations of S.cerevisiae Hsp82 and C.albicans Hsp90 are at the very least similar. It will be of considerable interest to compare the ubiquitination and subsequent degradation of Hsp90 from the two yeast species, and to discover if the two proteins are recognised and ubiquitinated by the same processes.
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