Engineered interfaces of an AAA+ ATPase reveal a new nucleotide-dependent coordination mechanism.

ABSTRACT: Homohexameric ring AAA(+) ATPases are found in all kingdoms of life and are involved in all cellular processes. To accommodate the large spectrum of substrates, the conserved AAA(+) core has become specialized through the insertion of specific substrate-binding motifs. Given their critical roles in cellular function, understanding the nucleotide-driven mechanisms of action is of wide importance. For one type of member AAA(+) protein (phage shock protein F, PspF), we identified and established the functional significance of strategically placed arginine and glutamate residues that form interacting pairs in response to nucleotide binding. We show that these interactions are critical for "cis" and "trans" subunit communication, which support coordination between subunits for nucleotide-depend

SUBMITTER: Joly N 

PROVIDER: S-EPMC2865273 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature