Unit:
ΠΜΣ Μικροβιακή ΒιοτεχνολογίαLibrary of the School of Science
Supervisors info:
Καθηγητής Μιλτιάδης Α. Τύπας, Καθηγήτρια Αμαλία Καραγκούνη – Κύρτσου, Καθηγητής Γεώργιος Διαλλινάς
Original Title:
Εισοσωμικές πρωτεΐνες: μελέτη των σχέσεων δομής – λειτουργίας στον υφομύκητα Aspergillus nidulans
Translated title:
Eisosomal proteins: study of structure-function relationships in the hyphomycete Aspergillus nidulans
Summary:
The plasma membrane components are not randomly distributed across the
membrane, however they are compartmentalized in specific domains. The three
better studied membrane compartment in the yeast fungus Saccharomyces
cerevisiae are: the Membrane Compartment of Can1 (MCC), the Membrane
Compartment of Pma1 (MCP) and the Membrane Compartment of TORC2 (MCT). The
normal compartmentalization of the consisting proteins of MCC is dependent on
the presence of a multi-protein compex, the eisosome. The main organizer of
eisosomes in S. cerevisiae is the Pil1 protein, which consists of the
semi-crescent BAR domain (Bin/Amphyphisin/Rvs). BAR domain proteins are
homodimers and are important for the stabilization and maintenance of membrane
curvature, while they are related to several cell functions such as
clathrin-mediated endocytosis. The homologue protein to Pil1 in the hyphomycete
Aspergillus nidulans is PilA. In this study, the impact of specific amino-acid
residue substitutions in the BAR domain on the protein’s functionality were
examined. The protein markers used to determine the functionality of PilA were
the eisosomal proteins AnNce102 and PilB. Our results show that specific
amino-acid residues of the BAR domain are important for the normal dimerization
of the protein, and for its interaction with the plasma membrane of the cell.
Keywords:
Aspergillus, PilA, Eisosomes, BAR proteins
Number of references:
165
