Ciamak Ghazaei - Assistant Professor, Mohaghegh Ardabili University

ATPases Associated with diverse cellular Activities (AAA+) proteases belong to a superfamily of proteins that form a major part of bacterial protein quality control network. They participate in the degradation of misfolded, aggregated or damaged proteins, and play an important role in the turnover of regulatory proteins, thus controlling protein homeostasis. Members of this superfamily contain highly conserved ATPase module, which includes core domain with canonical Walker A and B motifs is used for ATP binding and hydrolysis, and catalytic module. Bacterial AAA+ proteins typically form hexameric complexes, and undergo conformational changes upon binding and hydrolysis of ATP to unfold and remodel protein substrates, as well as DNA/RNA, or multicomponent complexes. Many AAA+ proteins also function as chaperones and are essential for protein quality control in the bacterial cell. Bacterial AAA+ proteins exhibit structural and functional variability that allows the processing of a wide range of target substrates. This functional diversity is further increased by a number partner proteins and cofactors that work together with AAA+ proteins in bacterial cells.

AAA+ proteins,Bacterial protein, Walker A and B, ATP, Substrates