Results 41 to 50 of about 63,350 (232)

TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. [PDF]

, 2015
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family.
Corbett, Kevin D, Moeller, Arne, Rosenberg, Scott C, Speir, Jeffrey A, Su, Tiffany Y, Ye, Qiaozhen   +5 more
core   +2 more sources

Polypeptide Translocation by the AAA+ ClpXP Protease Machine

Chemistry & Biology, 2009
In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite major differences in side-chain chirality, size, and ...
Barkow, Sarah R., Levchenko, Igor, Baker, Tania, Sauer, Robert T   +3 more
openaire   +4 more sources

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation. [PDF]

, 2019
The 26S proteasome is essential for proteostasis and the regulation of vital processes through ATP-dependent degradation of ubiquitinated substrates. To accomplish the multi-step degradation process, the proteasomes regulatory particle, consisting of lid
Aufderheide, Bard, Bard, Bard, Bashore, Beckwith, Dambacher, de la Peña, Ding, Dong, Eisele, Elsasser, Finley, Glickman, Glickman, Goldstein, Groll, Hershko, Kachroo, Lander, Lasker, Longtine, Matyskiela, Myers, Nemec, Peth, Prakash, Rubin, Smith, Sone, Tomko, Unverdorben, Verma, VerPlank, VerPlank, Wehmer, Wendler, Wenzel, Worden, Worden, Yao, Zhu, Śledź   +42 more
core   +1 more source

Engineering fluorescent protein substrates for the AAA+ Lon protease [PDF]

Protein Engineering Design and Selection, 2013
AAA+ proteases, such as Escherichia coli Lon, recognize protein substrates by binding to specific peptide degrons and then unfold and translocate the protein into an internal degradation chamber for proteolysis. For some AAA+ proteases, attaching specific degrons to the N- or C-terminus of green fluorescent protein (GFP) generates useful substrates ...
Matthew L, Wohlever, Andrew R, Nager, Tania A, Baker, Robert T, Sauer   +3 more
openaire   +2 more sources

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

eLife, 2020
ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the E.
Xue Fei, Tristan A Bell, Simon Jenni, Benjamin M Stinson, Tania A Baker, Stephen C Harrison, Robert T Sauer   +6 more
doaj   +1 more source

A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria. [PDF]

, 2011
To broadly explore mitochondrial structure and function as well as the communication of mitochondria with other cellular pathways, we constructed a quantitative, high-density genetic interaction map (the MITO-MAP) in Saccharomyces cerevisiae.
Cassidy-Stone, Ann, Collins, Sean R, Devay, Rachel M, Hoppins, Suzanne, Hummel, Eric, Lackner, Laura L, Nunnari, Jodi, Schuldiner, Maya, Weissman, Jonathan S, Westermann, Benedikt   +9 more
core   +2 more sources

Sculpting the Proteome with AAA+ Proteases and Disassembly Machines [PDF]

Cell, 2004
Machines of protein destruction-including energy-dependent proteases and disassembly chaperones of the AAA(+) ATPase family-function in all kingdoms of life to sculpt the cellular proteome, ensuring that unnecessary and dangerous proteins are eliminated and biological responses to environmental change are rapidly and properly regulated.
Sauer, Robert T., Bolon, Daniel N., Burton, Briana M., Burton, Randall E., Flynn, Julia M., Grant, Robert A., Hersch, Greg L., Joshi, Shilpa A., Kenniston, Jon A., Levchenko, Igor, Neher, Saskia B., Oakes, Elizabeth S.C., Siddiqui, Samia M., Wah, David A., Baker, Tania A.   +14 more
openaire   +2 more sources

Membrane protein degradation by AAA proteases in mitochondria

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2002
The inner membrane of mitochondria is one of the protein's richest cellular membranes. The biogenesis of the respiratory chain and ATP-synthase complexes present in this membrane is an intricate process requiring the coordinated function of various membrane-bound proteins including protein translocases and assembly factors.
Arnold, I., Langer, T.
openaire   +3 more sources

Autocatalytic Processing of m-AAA Protease Subunits in Mitochondria [PDF]

Molecular Biology of the Cell, 2009
m-AAA proteases are ATP-dependent proteolytic machines in the inner membrane of mitochondria which are crucial for the maintenance of mitochondrial activities. Conserved nuclear-encoded subunits, termed paraplegin, Afg3l1, and Afg3l2, form various isoenzymes differing in their subunit composition in mammalian mitochondria. Mutations in different m-AAA
Koppen, M., Bonn, F., Ehses, S., Langer, T.   +3 more
openaire   +3 more sources

A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine

Nature Communications, 2023
Many AAA+ (ATPases associated with diverse cellular activities) proteins function as protein or DNA remodelers by threading the substrate through the central pore of their hexameric assemblies.
Shanshan Li, Kan-Yen Hsieh, Chiao-I Kuo, Tzu-Chi Lin, Szu-Hui Lee, Yi-Ru Chen, Chun-Hsiung Wang, Meng-Ru Ho, See-Yeun Ting, Kaiming Zhang, Chung-I Chang   +10 more
doaj   +1 more source