From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins

Biochemical Society Transactions
Teru OguraKunitoshi Yamanaka

Abstract

AAA (ATPase associated with various cellular activities) proteins remodel substrate proteins and protein complexes upon ATP hydrolysis. Substrate remodelling is diverse, e.g. proteolysis, unfolding, disaggregation and disassembly. In the oligomeric ring of the AAA protein, there is a conserved aromatic residue which lines the central pore. Functional analysis indicates that this conserved residue in AAA proteases is involved in threading unfolded polypeptides. Katanin and spastin have microtubule-severing activity. These AAA proteins also possess a conserved aromatic residue at the central pore, suggesting its importance in their biological activity. We have constructed pore mutants of these AAA proteins and have obtained in vivo and in vitro results indicating the functional importance of the pore motif. Degradation of casein by the Escherichia coli AAA protease, FtsH, strictly requires ATP hydrolysis. We have constructed several chimaeric proteases by exchanging domains of FtsH and its homologues from Caenorhabditis elegans mitochondria, and examined their ATPase and protease activities in vitro. Interestingly, it has been found that some chimaeras are able to degrade casein in an ATP-independent manner. The proteolysis is su...Continue Reading

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Citations

Jan 11, 2012·Proceedings of the National Academy of Sciences of the United States of America·Cecilia BebeacuaPaul S Freemont
Sep 9, 2008·Journal of Bacteriology·Chen Katz, Eliora Z Ron
Sep 13, 2011·Biochimica Et Biophysica Acta·Nicolas JolyXiaodong Zhang
Jun 22, 2011·Biochimica Et Biophysica Acta·Chunxia ZhaoSidney W Whiteheart
Mar 4, 2010·The Journal of Biological Chemistry·Nicolas Joly, Martin Buck
Apr 19, 2019·JMIR Mental Health·Joseph Fordham, Christopher Ball
Jan 23, 2008·Biochemical Society Transactions·Andreas FörsterR John Mayer

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