Theo Papakonstantinou

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Subunit 8 of yeast mitochondrial ATP synthase is a small hydrophobic component of the membrane-associated F0 sector. Structure/function relations in subunit 8 were studied by focusing on three structural domains: a highly conserved NH2-terminal region, a central hydrophobic region (previously suggested to be a transmembrane stem), and a COOH-terminal region(More)
The transforming growth factor-beta (TGF-beta) superfamily member, activin A, plays a central role in the regulation of multiple physiological processes including cell differentiation, mitogenesis, embryogenesis, apoptosis and inflammation. In normal cells, activin A signalling is regulated to maintain cellular and tissue health and suppress tumour growth.(More)
Subunit 8 (Y8) is a component of the proton channel of yeast (Saccharomyces cerevisiae) mitochondrial ATP synthase (mtATPase), whose function in the complex remains to be precisely defined. Y8 variants truncated at residue 46 (Lys47-->STP), or in which each of three conserved C-terminal amino acid residues (Arg37, Arg42 and Lys47) were substituted with(More)
Each of three conserved positively-charged residues in the C-terminal region of subunit 8 of yeast (Saccharomyces cerevisiae) mitochondrial ATP synthase was replaced with isoleucine. The assembly and functional properties of the resulting variants (substituted at Arg-37, Arg-42 and Lys-47) were examined using in-vitro systems to assay import into isolated(More)
The ICA512/IA-2 molecule, a protein with similarity to receptor-type protein tyrosine phosphatases, was discovered during studies to identify autoantigens in Type 1 diabetes. The biological function of ICA512/IA-2 is unknown. We describe striking effects of ICA512/IA-2 on viability and growth of both yeast cells and cultured mammalian cells. In transformed(More)
Subunit 8 (Y8) of yeast mitochondrial ATP synthase (mtATPase) is a hydrophobic component of the membrane Fo sector. Encoded by the mitochondrial aap1 gene, Y8 is a 48-amino-acid polypeptide having a central hydrophobic domain (CHD) spanning 19 residues. Site-directed mutagenesis was carried out on a nuclear code-equivalent gene encoding Y8, to introduce(More)
Pichia pastoris is a popular host organism for expressing heterologous proteins, and various expression vectors for this yeast are currently available. Recently, vectors containing novel dominant antibiotic resistance markers have become a strong and developing field of research for this methylotropic yeast strain. We have developed new P. pastoris(More)
A molecular genetic approach has been used to test the proposition that the central hydrophobic domain of yeast mitochondrial ATP synthase subunit 8 represents a transmembrane stem in contact with the lipid bilayer. The rationale for this approach is the general inability of membrane bilayers to accomodate unshielded charged residues of polypeptide chains.(More)
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