IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Role of the N-terminal domain of the regulatory subunit of protein kinase A from fungi in dimerization and tethering to proteins
Autor/es:
MORENO, SILVIA; GALELLO, FIORELLA, RINALDI, JIMENA, GONZÁLEZ-BARDECI, NICOLÁS, PEREYRA, ELBA, ROSSI, SILVIA
Lugar:
Oslo, Noruega
Reunión:
Congreso; 3rd International Meeting on Anchored cAMP Signalling Pathways, Oslo, Norway; 2010
Resumen:
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Among fungi both ascomycetes and
basidiomycetes have only one isoform of regulatory subunit (R) of PKA, while
zygomycetes have four isoforms. A bioinformatic comparison of the divergent
amino termini of the R subunits from fungi with those of mammals showed a
conserved region with characteristics of dimerization domains (D/D) both in
primary and secondary structure. A subfillum of ascomycetes, exemplified by Neurospora
crassa, lacked this region and showed to have a monomeric R subunit. We studied
in detail the N-terminus from Saccharomyces cerevisiae (ascomycete) and Mucor
circinelloides (zygomycete). In the S.cerevisiae dimeric R (Bcy1) subunit the
deletion of the D/D yielded a monomeric isoform. A comparison of the D/D region of Bcy1 and the four R subunits from M. circinelloides with the
D/D domains of RI and RII predicts possible interacting surfaces for these subunits
with other proteins. By pull-down assay Bcy1 was shown to interact with
D-AKAP2. The addition of the permeable version of Ht-31 to M.circinelloides
growth medium, had significant phenotypic consequences. Possible interactors of
Bcy1 were selected making theoretical predictions of putative AKAPs from the
yeast genome *. Determinants and
strength of the interactions with Bcy-1 and the role of the N-terminus in these
interactions were assayed by peptide array.