Results 221 to 230 of about 401,347 (255)
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Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease

Nature, 1999
The AAA domain, a conserved Walker-type ATPase module, is a feature of members of the AAA family of proteins, which are involved in many cellular processes, including vesicular transport, organelle biogenesis, microtubule rearrangement and protein degradation. The function of the AAA domain, however, has not been explained.
Leonhard, K.   +3 more
openaire   +3 more sources

Nucleotide-dependent substrate recognition by the AAA+ HslUV protease

Nature Structural & Molecular Biology, 2005
ATP-dependent protein degradation is controlled principally by substrate recognition. The AAA+ HslU ATPase is thought to bind protein substrates, denature them, and translocate the unfolded polypeptide into the HslV peptidase. The lack of well-behaved high-affinity substrates for HslUV (ClpYQ) has hampered understanding of the rules and mechanism of ...
Randall E, Burton   +2 more
openaire   +2 more sources

ClpP: A structurally dynamic protease regulated by AAA+ proteins

Journal of Structural Biology, 2012
Proteolysis is an important process for many aspects of bacterial physiology. Clp proteases carry out a large proportion of protein degradation in bacteria. These enzymes assemble in complexes that combine the protease ClpP and the unfoldase, ClpA or ClpX.
John A, Alexopoulos   +2 more
openaire   +2 more sources

The Lon AAA+ Protease

2013
As the first ATP-dependent protease to be identified, Lon holds a special place in the history of cellular biology. In fact, the concept of ATP-dependent protein degradation was established through the findings that led to the discovery of Lon. Therefore, this chapter begins with a historical perspective, describing the milestones that led to the ...
openaire   +2 more sources

AAA proteases: cellular machines for degrading membrane proteins

Trends in Biochemical Sciences, 2000
AAA proteases are a conserved class of ATP-dependent proteases that mediate the degradation of membrane proteins in bacteria, mitochondria and chloroplasts. They combine proteolytic and chaperone-like activities and thus form a membrane-integrated quality-control system.
openaire   +3 more sources

Protein knots provide mechano-resilience to an AAA+ protease-mediated proteolysis with profound ATP energy expenses.

Biochimica et Biophysica Acta - Proteins and Proteomics, 2019
Knotted proteins are some of the most fascinating examples of how linear polypeptide chains can achieve intricate topological arrangements efficiently and spontaneously.
M. K. Sriramoju, Yen-Ning Chen, S. Hsu
semanticscholar   +1 more source

Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases

Nature Reviews Microbiology, 2009
Members of the AAA+ protein superfamily contribute to many diverse aspects of protein homeostasis in prokaryotic cells. As a fundamental component of numerous proteolytic machines in bacteria, AAA+ proteins play a crucial part not only in general protein quality control but also in the regulation of developmental programmes, through the controlled ...
Kirstein, Janine.   +3 more
openaire   +2 more sources

Structural basis for prohibitin-mediated regulation of mitochondrial m-AAA protease

bioRxiv
Dingyi Luo   +6 more
semanticscholar   +1 more source

The i-AAA protease

2013
Wai, T., Langer, T.
openaire   +2 more sources

AAA+ Proteases

RCSB Protein Data Bank, 2006
openaire   +1 more source

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